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Q9M884

- MPI1_ARATH

UniProt

Q9M884 - MPI1_ARATH

Protein

Mannose-6-phosphate isomerase 1

Gene

PMI1

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 99 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions. Involved in the ascorbic acid (AsA) biosynthesis. Required during the endosperm development.2 Publications

    Catalytic activityi

    D-mannose 6-phosphate = D-fructose 6-phosphate.

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Enzyme regulationi

    Inhibited by EDTA, Zn2+, Cd2+, Co2+, p-chloromercuribenzoate and L-ascorbic acid (AsA).1 Publication

    Kineticsi

    1. KM=41.3 µM for mannose-6-phosphate1 Publication

    Vmax=1.89 µmol/min/mg enzyme with mannose-6-phosphate as substrate1 Publication

    pH dependencei

    Optimum pH is 7.5.1 Publication

    Temperature dependencei

    Optimum temperature is 52 degrees Celsius.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi124 – 1241ZincBy similarity
    Metal bindingi126 – 1261ZincBy similarity
    Metal bindingi151 – 1511ZincBy similarity
    Metal bindingi288 – 2881ZincBy similarity
    Active sitei307 – 3071By similarity

    GO - Molecular functioni

    1. mannose-6-phosphate isomerase activity Source: TAIR
    2. zinc ion binding Source: InterPro

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro
    2. embryo development ending in seed dormancy Source: TAIR
    3. GDP-mannose biosynthetic process Source: UniProtKB-UniPathway
    4. response to cadmium ion Source: UniProtKB
    5. response to cobalt ion Source: UniProtKB
    6. response to L-ascorbic acid Source: UniProtKB
    7. response to light stimulus Source: UniProtKB
    8. response to zinc ion Source: UniProtKB

    Keywords - Molecular functioni

    Isomerase

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciARA:AT3G02570-MONOMER.
    MetaCyc:AT3G02570-MONOMER.
    ReactomeiREACT_190862. Synthesis of GDP-mannose.
    UniPathwayiUPA00126; UER00423.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mannose-6-phosphate isomerase 1 (EC:5.3.1.8)
    Alternative name(s):
    Phosphohexomutase 1
    Phosphomannose isomerase 1
    Short name:
    PMI1
    Protein MATERNAL EFFECT EMBRYO ARREST 31
    Gene namesi
    Name:PMI1
    Synonyms:MEE31
    Ordered Locus Names:At3g02570
    ORF Names:F16B3.20
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 3

    Organism-specific databases

    TAIRiAT3G02570.

    Pathology & Biotechi

    Disruption phenotypei

    Endosperm development arrested.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 432432Mannose-6-phosphate isomerase 1PRO_0000420339Add
    BLAST

    Proteomic databases

    PaxDbiQ9M884.
    PRIDEiQ9M884.

    Expressioni

    Tissue specificityi

    Constitutively expressed in both vegetative and reproductive organs under normal growth conditions (at protein level).1 Publication

    Inductioni

    By light (at the protein level). Down-regulated by dark (at the protein level). Down-regulated by DCMU, an exogenous photosynthesis inhibitor.1 Publication

    Gene expression databases

    GenevestigatoriQ9M884.

    Interactioni

    Protein-protein interaction databases

    IntActiQ9M884. 1 interaction.
    STRINGi3702.AT3G02570.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9M884.
    SMRiQ9M884. Positions 19-426.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1482.
    HOGENOMiHOG000241277.
    InParanoidiQ9M884.
    KOiK01809.
    OMAiWITENPK.
    PhylomeDBiQ9M884.

    Family and domain databases

    Gene3Di2.60.120.10. 3 hits.
    InterProiIPR001250. Man6P_Isoase-1.
    IPR016305. Mannose-6-P_Isomerase.
    IPR018050. Pmannose_isomerase-type1_CS.
    IPR014710. RmlC-like_jellyroll.
    IPR011051. RmlC_Cupin.
    [Graphical view]
    PANTHERiPTHR10309. PTHR10309. 1 hit.
    PfamiPF01238. PMI_typeI. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001480. Mannose-6-phosphate_isomerase. 1 hit.
    PRINTSiPR00714. MAN6PISMRASE.
    SUPFAMiSSF51182. SSF51182. 1 hit.
    TIGRFAMsiTIGR00218. manA. 1 hit.
    PROSITEiPS00965. PMI_I_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9M884-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEIATVVKAN GGCEADRRRL RRLRCSVKDY DWGKIGSDSL VYRVYAANSD    50
    YEIDPTRPYA ELWMGTHESG PSYLEDADGS NGVTLRSWIT ENPKSLGNRV 100
    LEKWGCDLPF LFKVLSVARP LSIQAHPDKK LAKKMHKAHP NLYKDDNHKP 150
    EMALAYTQFE ALCGFIPLQE LKSVIRAIPE IEELVGSEEA NQVFCITEHD 200
    EEKVKSVVRT IFTLLMSADA DTTKKIVSKL KRRLHMESQE RQLTDKERLV 250
    LKLEKQYPND IGVISAFFFN YVKLNPGEAL YLGANEPHAY LFGECLEVMA 300
    TSDNVVRAGL TSKPLDIQTL CSMLSYKLGY PEILKGTRIR PYITRYLPPF 350
    EEFEVDLCDL PSGASTVFPS VPGPSLLLVL QGEGRMSTEA SADGISMGDV 400
    LFVPADTEIH LRSSSDLKLY RAGINSRFLF PL 432
    Length:432
    Mass (Da):48,566
    Last modified:October 1, 2000 - v1
    Checksum:i9BF364B9BCF8FC9B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC021640 Genomic DNA. Translation: AAF32464.1.
    CP002686 Genomic DNA. Translation: AEE73831.1.
    AY070447 mRNA. Translation: AAL49850.1.
    AY096564 mRNA. Translation: AAM20214.1.
    RefSeqiNP_186906.1. NM_111125.3.
    UniGeneiAt.18813.
    At.24147.

    Genome annotation databases

    EnsemblPlantsiAT3G02570.1; AT3G02570.1; AT3G02570.
    GeneIDi820656.
    KEGGiath:AT3G02570.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC021640 Genomic DNA. Translation: AAF32464.1 .
    CP002686 Genomic DNA. Translation: AEE73831.1 .
    AY070447 mRNA. Translation: AAL49850.1 .
    AY096564 mRNA. Translation: AAM20214.1 .
    RefSeqi NP_186906.1. NM_111125.3.
    UniGenei At.18813.
    At.24147.

    3D structure databases

    ProteinModelPortali Q9M884.
    SMRi Q9M884. Positions 19-426.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9M884. 1 interaction.
    STRINGi 3702.AT3G02570.1-P.

    Proteomic databases

    PaxDbi Q9M884.
    PRIDEi Q9M884.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT3G02570.1 ; AT3G02570.1 ; AT3G02570 .
    GeneIDi 820656.
    KEGGi ath:AT3G02570.

    Organism-specific databases

    TAIRi AT3G02570.

    Phylogenomic databases

    eggNOGi COG1482.
    HOGENOMi HOG000241277.
    InParanoidi Q9M884.
    KOi K01809.
    OMAi WITENPK.
    PhylomeDBi Q9M884.

    Enzyme and pathway databases

    UniPathwayi UPA00126 ; UER00423 .
    BioCyci ARA:AT3G02570-MONOMER.
    MetaCyc:AT3G02570-MONOMER.
    Reactomei REACT_190862. Synthesis of GDP-mannose.

    Miscellaneous databases

    PROi Q9M884.

    Gene expression databases

    Genevestigatori Q9M884.

    Family and domain databases

    Gene3Di 2.60.120.10. 3 hits.
    InterProi IPR001250. Man6P_Isoase-1.
    IPR016305. Mannose-6-P_Isomerase.
    IPR018050. Pmannose_isomerase-type1_CS.
    IPR014710. RmlC-like_jellyroll.
    IPR011051. RmlC_Cupin.
    [Graphical view ]
    PANTHERi PTHR10309. PTHR10309. 1 hit.
    Pfami PF01238. PMI_typeI. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001480. Mannose-6-phosphate_isomerase. 1 hit.
    PRINTSi PR00714. MAN6PISMRASE.
    SUPFAMi SSF51182. SSF51182. 1 hit.
    TIGRFAMsi TIGR00218. manA. 1 hit.
    PROSITEi PS00965. PMI_I_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
      Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
      , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
      Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    2. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    3. "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.
    4. "Genetic and molecular identification of genes required for female gametophyte development and function in Arabidopsis."
      Pagnussat G.C., Yu H.-J., Ngo Q.A., Rajani S., Mayalagu S., Johnson C.S., Capron A., Xie L.-F., Ye D., Sundaresan V.
      Development 132:603-614(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    5. "Arabidopsis phosphomannose isomerase 1, but not phosphomannose isomerase 2, is essential for ascorbic acid biosynthesis."
      Maruta T., Yonemitsu M., Yabuta Y., Tamoi M., Ishikawa T., Shigeoka S.
      J. Biol. Chem. 283:28842-28851(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, TISSUE SPECIFICITY, INDUCTION.
    6. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiMPI1_ARATH
    AccessioniPrimary (citable) accession number: Q9M884
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 28, 2012
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 99 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