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Q9M9P3

- UGPA2_ARATH

UniProt

Q9M9P3 - UGPA2_ARATH

Protein

Probable UTP--glucose-1-phosphate uridylyltransferase 2

Gene

At3g03250

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Plays a central role as a glucosyl donor in cellular metabolic pathways.By similarity

    Catalytic activityi

    UTP + alpha-D-glucose 1-phosphate = diphosphate + UDP-glucose.

    GO - Molecular functioni

    1. UTP:glucose-1-phosphate uridylyltransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. callose deposition in cell wall Source: TAIR
    2. cellular response to phosphate starvation Source: TAIR
    3. pollen development Source: TAIR
    4. response to salt stress Source: TAIR
    5. sucrose metabolic process Source: TAIR

    Keywords - Molecular functioni

    Nucleotidyltransferase, Transferase

    Enzyme and pathway databases

    BioCyciARA:AT3G03250-MONOMER.
    MetaCyc:AT3G03250-MONOMER.
    ReactomeiREACT_180021. Glycogen synthesis.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable UTP--glucose-1-phosphate uridylyltransferase 2 (EC:2.7.7.9)
    Alternative name(s):
    UDP-glucose pyrophosphorylase 2
    Short name:
    UDPGP 2
    Short name:
    UGPase 2
    Gene namesi
    Ordered Locus Names:At3g03250
    ORF Names:T17B22.6
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 3

    Organism-specific databases

    TAIRiAT3G03250.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytosol Source: TAIR
    2. plasma membrane Source: TAIR
    3. pollen tube Source: TAIR

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 469468Probable UTP--glucose-1-phosphate uridylyltransferase 2PRO_0000185757Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiQ9M9P3.
    PRIDEiQ9M9P3.

    Expressioni

    Gene expression databases

    GenevestigatoriQ9M9P3.

    Interactioni

    Protein-protein interaction databases

    BioGridi6646. 1 interaction.

    Structurei

    Secondary structure

    1
    469
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi8 – 1710
    Beta strandi19 – 213
    Helixi23 – 3614
    Helixi46 – 483
    Turni54 – 563
    Beta strandi57 – 593
    Helixi60 – 623
    Helixi70 – 778
    Beta strandi80 – 867
    Helixi91 – 933
    Beta strandi96 – 983
    Helixi99 – 1013
    Beta strandi102 – 1054
    Helixi110 – 12516
    Beta strandi131 – 1355
    Turni137 – 1393
    Helixi140 – 1478
    Helixi148 – 1503
    Beta strandi153 – 1553
    Beta strandi157 – 1615
    Turni170 – 1734
    Helixi176 – 1794
    Helixi184 – 1863
    Helixi192 – 1943
    Helixi195 – 2028
    Helixi204 – 2096
    Beta strandi215 – 2206
    Helixi230 – 23910
    Beta strandi242 – 2498
    Helixi252 – 2543
    Beta strandi259 – 2635
    Beta strandi266 – 2705
    Helixi272 – 2743
    Helixi277 – 2793
    Helixi280 – 2845
    Beta strandi285 – 2884
    Beta strandi291 – 30010
    Helixi301 – 3099
    Beta strandi321 – 3244
    Beta strandi327 – 3304
    Helixi336 – 3427
    Beta strandi347 – 3504
    Helixi353 – 3553
    Helixi362 – 3698
    Beta strandi373 – 3764
    Beta strandi379 – 3824
    Beta strandi388 – 3903
    Beta strandi393 – 3964
    Helixi398 – 4003
    Helixi403 – 4086
    Beta strandi410 – 4123
    Beta strandi419 – 43012
    Beta strandi435 – 4439
    Beta strandi449 – 4524
    Beta strandi457 – 4604
    Helixi466 – 4683

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1Z90X-ray1.86A/B1-469[»]
    2ICXX-ray1.85A/B2-469[»]
    2ICYX-ray1.64A/B2-469[»]
    2Q4JX-ray1.86A/B1-469[»]
    ProteinModelPortaliQ9M9P3.
    SMRiQ9M9P3. Positions 7-469.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9M9P3.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the UDPGP type 1 family.Curated

    Phylogenomic databases

    eggNOGiCOG4284.
    HOGENOMiHOG000113618.
    InParanoidiQ9M9P3.
    KOiK00963.
    OMAiAIDVFSH.
    PhylomeDBiQ9M9P3.

    Family and domain databases

    Gene3Di3.90.550.10. 1 hit.
    InterProiIPR029044. Nucleotide-diphossugar_trans.
    IPR016267. UDPGP_trans.
    IPR002618. UDPGP_trans_fam.
    [Graphical view]
    PANTHERiPTHR11952. PTHR11952. 1 hit.
    PTHR11952:SF1. PTHR11952:SF1. 1 hit.
    PfamiPF01704. UDPGP. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000806. UDPGP. 1 hit.
    SUPFAMiSSF53448. SSF53448. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q9M9P3-1 [UniParc]FASTAAdd to Basket

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    MAATTENLPQ LKSAVDGLTE MSESEKSGFI SLVSRYLSGE AQHIEWSKIQ    50
    TPTDEIVVPY EKMTPVSQDV AETKNLLDKL VVLKLNGGLG TTMGCTGPKS 100
    VIEVRDGLTF LDLIVIQIEN LNNKYGCKVP LVLMNSFNTH DDTHKIVEKY 150
    TNSNVDIHTF NQSKYPRVVA DEFVPWPSKG KTDKEGWYPP GHGDVFPALM 200
    NSGKLDTFLS QGKEYVFVAN SDNLGAIVDL TILKHLIQNK NEYCMEVTPK 250
    TLADVKGGTL ISYEGKVQLL EIAQVPDEHV NEFKSIEKFK IFNTNNLWVN 300
    LKAIKKLVEA DALKMEIIPN PKEVDGVKVL QLETAAGAAI RFFDNAIGVN 350
    VPRSRFLPVK ASSDLLLVQS DLYTLVDGFV TRNKARTNPS NPSIELGPEF 400
    KKVATFLSRF KSIPSIVELD SLKVSGDVWF GSSIVLKGKV TVAAKSGVKL 450
    EIPDRAVVEN KNINGPEDL 469
    Length:469
    Mass (Da):51,738
    Last modified:October 1, 2000 - v1
    Checksum:iD0B70B92A2372820
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti187 – 1871W → R in AAK32773. (PubMed:14593172)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC012328 Genomic DNA. Translation: AAF26102.1.
    CP002686 Genomic DNA. Translation: AEE73917.1.
    AY035071 mRNA. Translation: AAK59576.1.
    AY059148 mRNA. Translation: AAL15254.1.
    AF361605 mRNA. Translation: AAK32773.1.
    RefSeqiNP_186975.1. NM_111195.3.
    UniGeneiAt.24250.

    Genome annotation databases

    EnsemblPlantsiAT3G03250.1; AT3G03250.1; AT3G03250.
    GeneIDi821313.
    KEGGiath:AT3G03250.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC012328 Genomic DNA. Translation: AAF26102.1 .
    CP002686 Genomic DNA. Translation: AEE73917.1 .
    AY035071 mRNA. Translation: AAK59576.1 .
    AY059148 mRNA. Translation: AAL15254.1 .
    AF361605 mRNA. Translation: AAK32773.1 .
    RefSeqi NP_186975.1. NM_111195.3.
    UniGenei At.24250.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1Z90 X-ray 1.86 A/B 1-469 [» ]
    2ICX X-ray 1.85 A/B 2-469 [» ]
    2ICY X-ray 1.64 A/B 2-469 [» ]
    2Q4J X-ray 1.86 A/B 1-469 [» ]
    ProteinModelPortali Q9M9P3.
    SMRi Q9M9P3. Positions 7-469.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 6646. 1 interaction.

    Proteomic databases

    PaxDbi Q9M9P3.
    PRIDEi Q9M9P3.

    Protocols and materials databases

    DNASUi 821313.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT3G03250.1 ; AT3G03250.1 ; AT3G03250 .
    GeneIDi 821313.
    KEGGi ath:AT3G03250.

    Organism-specific databases

    TAIRi AT3G03250.

    Phylogenomic databases

    eggNOGi COG4284.
    HOGENOMi HOG000113618.
    InParanoidi Q9M9P3.
    KOi K00963.
    OMAi AIDVFSH.
    PhylomeDBi Q9M9P3.

    Enzyme and pathway databases

    BioCyci ARA:AT3G03250-MONOMER.
    MetaCyc:AT3G03250-MONOMER.
    Reactomei REACT_180021. Glycogen synthesis.

    Miscellaneous databases

    EvolutionaryTracei Q9M9P3.

    Gene expression databases

    Genevestigatori Q9M9P3.

    Family and domain databases

    Gene3Di 3.90.550.10. 1 hit.
    InterProi IPR029044. Nucleotide-diphossugar_trans.
    IPR016267. UDPGP_trans.
    IPR002618. UDPGP_trans_fam.
    [Graphical view ]
    PANTHERi PTHR11952. PTHR11952. 1 hit.
    PTHR11952:SF1. PTHR11952:SF1. 1 hit.
    Pfami PF01704. UDPGP. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000806. UDPGP. 1 hit.
    SUPFAMi SSF53448. SSF53448. 1 hit.
    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. "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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    5. "X-ray structure of gene product from Arabidopsis thaliana At3g03250, a putative UDP-glucose pyrophosphorylase."
      Center for eukaryotic structural genomics (CESG)
      Submitted (APR-2005) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 1-469.

    Entry informationi

    Entry nameiUGPA2_ARATH
    AccessioniPrimary (citable) accession number: Q9M9P3
    Secondary accession number(s): Q9ASY1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2006
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 92 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3