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Q9SA34

- IMDH2_ARATH

UniProt

Q9SA34 - IMDH2_ARATH

Protein

Inosine-5'-monophosphate dehydrogenase 2

Gene

At1g16350

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 113 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.UniRule annotation

    Catalytic activityi

    Inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH.UniRule annotation

    Cofactori

    Potassium.UniRule annotation

    Enzyme regulationi

    Mycophenolic acid (MPA) is a non-competitive inhibitor that prevents formation of the closed enzyme conformation by binding to the same site as the amobile flap. In contrast, mizoribine monophosphate (MZP) is a competitive inhibitor that induces the closed conformation. MPA is a potent inhibitor of mammalian IMPDHs but a poor inhibitor of the bacterial enzymes. MZP is a more potent inhibitor of bacterial IMPDH.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi316 – 3161Potassium; via carbonyl oxygenUniRule annotation
    Metal bindingi318 – 3181Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei319 – 3191IMPUniRule annotation
    Active sitei321 – 3211Thioimidate intermediateUniRule annotation
    Metal bindingi321 – 3211Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei429 – 4291IMPUniRule annotation
    Metal bindingi488 – 4881Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
    Metal bindingi489 – 4891Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
    Metal bindingi490 – 4901Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi264 – 2663NADUniRule annotation
    Nucleotide bindingi314 – 3163NADUniRule annotation

    GO - Molecular functioni

    1. IMP dehydrogenase activity Source: UniProtKB-HAMAP
    2. metal ion binding Source: UniProtKB-HAMAP
    3. nucleotide binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. GMP biosynthetic process Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    GMP biosynthesis, Purine biosynthesis

    Keywords - Ligandi

    Metal-binding, NAD, Potassium

    Enzyme and pathway databases

    BioCyciARA:AT1G16350-MONOMER.
    UniPathwayiUPA00601; UER00295.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Inosine-5'-monophosphate dehydrogenase 2UniRule annotation (EC:1.1.1.205UniRule annotation)
    Short name:
    IMP dehydrogenase 2UniRule annotation
    Short name:
    IMPD 2UniRule annotation
    Short name:
    IMPDH 2UniRule annotation
    Gene namesi
    Ordered Locus Names:At1g16350
    ORF Names:F3O9.15
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 1

    Organism-specific databases

    TAIRiAT1G16350.

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytosol Source: TAIR

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 PublicationUniRule annotation
    Chaini2 – 502501Inosine-5'-monophosphate dehydrogenase 2PRO_0000093687Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiQ9SA34.
    PRIDEiQ9SA34.

    Expressioni

    Gene expression databases

    GenevestigatoriQ9SA34.

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    BioGridi23444. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9SA34.
    SMRiQ9SA34. Positions 5-502.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini166 – 22560CBSUniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni354 – 3563IMP bindingUniRule annotation
    Regioni377 – 3782IMP bindingUniRule annotation
    Regioni401 – 4055IMP bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the IMPDH/GMPR family.UniRule annotation
    Contains 1 CBS domain.UniRule annotation

    Keywords - Domaini

    CBS domain

    Phylogenomic databases

    eggNOGiCOG0516.
    HOGENOMiHOG000165752.
    InParanoidiQ9SA34.
    KOiK00088.
    OMAiYMRPAPR.
    PhylomeDBiQ9SA34.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_01964. IMPDH.
    InterProiIPR013785. Aldolase_TIM.
    IPR005990. IMP_DH.
    IPR015875. IMP_DH/GMP_Rdtase_CS.
    IPR001093. IMP_DH_GMPRt.
    [Graphical view]
    PANTHERiPTHR11911:SF6. PTHR11911:SF6. 1 hit.
    PfamiPF00478. IMPDH. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000130. IMPDH. 1 hit.
    TIGRFAMsiTIGR01302. IMP_dehydrog. 1 hit.
    PROSITEiPS00487. IMP_DH_GMP_RED. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9SA34-1 [UniParc]FASTAAdd to Basket

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    MSGFEDGFSA EKLFSQGYSY TYDDVIFLPH FIDFSTDAVS LSTRLSKRVP    50
    LSIPCVASPM DTVSESHMAA AMAALGGIGI VHYNCDIDTQ ASVIRHAKSL 100
    QVPIASDAVF KCPEHQIGSV DDFGPSSFVF VSQTGTLTPK LLGYVSKSEW 150
    SSMKDDQKEV KIYDYMKSCE NKDYYVPWDI DLDKIEAVLE DKQKGFVVLE 200
    KEGETVNVVT KDDVERVKGY PKLGSGTVGA DKKWMVGAAI GTRESDKERL 250
    EHLVKAGANV VVLDSSQGNS IYQLEMIKYV KNTYPELDVV GGNVVTMYQA 300
    ENLIKAGVDG LRVGMGSGSI CTTQEVCAVG RGQATAVYKV STLAAQHGVP 350
    VIADGGISNS GHIVKALVLG ASTVMMGSFL AGSTEAPGAY EYRNGRRVKK 400
    YRGMGSLEAM TKGSDQRYLG DTAKLKIAQG VVGAVADKGS VLKFIPYTMH 450
    AVKQGFQDLG ASSLQSAHEL LRDNTLRLEA RTGAAQIEGG IHGLVSYEKK 500
    SF 502
    Length:502
    Mass (Da):54,051
    Last modified:May 1, 2000 - v1
    Checksum:iFB87D84160818310
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC006341 Genomic DNA. Translation: AAD34687.1.
    CP002684 Genomic DNA. Translation: AEE29441.1.
    PIRiF86298.
    RefSeqiNP_173085.1. NM_101501.2.
    UniGeneiAt.41887.

    Genome annotation databases

    EnsemblPlantsiAT1G16350.1; AT1G16350.1; AT1G16350.
    GeneIDi838204.
    KEGGiath:AT1G16350.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC006341 Genomic DNA. Translation: AAD34687.1 .
    CP002684 Genomic DNA. Translation: AEE29441.1 .
    PIRi F86298.
    RefSeqi NP_173085.1. NM_101501.2.
    UniGenei At.41887.

    3D structure databases

    ProteinModelPortali Q9SA34.
    SMRi Q9SA34. Positions 5-502.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 23444. 1 interaction.

    Proteomic databases

    PaxDbi Q9SA34.
    PRIDEi Q9SA34.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT1G16350.1 ; AT1G16350.1 ; AT1G16350 .
    GeneIDi 838204.
    KEGGi ath:AT1G16350.

    Organism-specific databases

    TAIRi AT1G16350.

    Phylogenomic databases

    eggNOGi COG0516.
    HOGENOMi HOG000165752.
    InParanoidi Q9SA34.
    KOi K00088.
    OMAi YMRPAPR.
    PhylomeDBi Q9SA34.

    Enzyme and pathway databases

    UniPathwayi UPA00601 ; UER00295 .
    BioCyci ARA:AT1G16350-MONOMER.

    Gene expression databases

    Genevestigatori Q9SA34.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    HAMAPi MF_01964. IMPDH.
    InterProi IPR013785. Aldolase_TIM.
    IPR005990. IMP_DH.
    IPR015875. IMP_DH/GMP_Rdtase_CS.
    IPR001093. IMP_DH_GMPRt.
    [Graphical view ]
    PANTHERi PTHR11911:SF6. PTHR11911:SF6. 1 hit.
    Pfami PF00478. IMPDH. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000130. IMPDH. 1 hit.
    TIGRFAMsi TIGR01302. IMP_dehydrog. 1 hit.
    PROSITEi PS00487. IMP_DH_GMP_RED. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
      Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
      , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
      Nature 408:816-820(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. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiIMDH2_ARATH
    AccessioniPrimary (citable) accession number: Q9SA34
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 2001
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 113 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