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P19595

- UGPA_SOLTU

UniProt

P19595 - UGPA_SOLTU

Protein

UTP--glucose-1-phosphate uridylyltransferase

Gene
N/A
Organism
Solanum tuberosum (Potato)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

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

    Catalytic activityi

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

    Cofactori

    Magnesium.

    Enzyme regulationi

    Inhibition by uncomplexed, free UTP.

    GO - Molecular functioni

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

    GO - Biological processi

    1. callose deposition in cell wall Source: EnsemblPlants/Gramene
    2. cellular response to phosphate starvation Source: EnsemblPlants/Gramene
    3. pollen development Source: EnsemblPlants/Gramene
    4. response to cadmium ion Source: EnsemblPlants/Gramene
    5. response to salt stress Source: EnsemblPlants/Gramene

    Keywords - Molecular functioni

    Nucleotidyltransferase, Transferase

    Keywords - Ligandi

    Magnesium

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    UTP--glucose-1-phosphate uridylyltransferase (EC:2.7.7.9)
    Alternative name(s):
    UDP-glucose pyrophosphorylase
    Short name:
    UDPGP
    Short name:
    UGPase
    OrganismiSolanum tuberosum (Potato)
    Taxonomic identifieri4113 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanum
    ProteomesiUP000011115: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: EnsemblPlants/Gramene
    2. plasma membrane Source: EnsemblPlants/Gramene
    3. pollen tube Source: EnsemblPlants/Gramene

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi263 – 2631K → Q: Significant decreased Vmax values. 1 Publication
    Mutagenesisi329 – 3291K → Q: Increased Km, Vmax like wild-type. 1 Publication
    Mutagenesisi367 – 3671K → Q: Almost complete loss of activity. 1 Publication
    Mutagenesisi409 – 4091K → Q: Activity almost like wild-type. 1 Publication
    Mutagenesisi410 – 4101K → Q: Activity almost like wild-type. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 477476UTP--glucose-1-phosphate uridylyltransferasePRO_0000185762Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PRIDEiP19595.

    Interactioni

    Subunit structurei

    Monomer.

    Structurei

    3D structure databases

    ProteinModelPortaliP19595.
    SMRiP19595. Positions 15-477.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the UDPGP type 1 family.Curated

    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.

    P19595-1 [UniParc]FASTAAdd to Basket

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    MATATTLSPA DAEKLNNLKS AVAGLNQISE NEKSGFINLV GRYLSGEAQH    50
    IDWSKIQTPT DEVVVPYDKL APLSEDPAET KKLLDKLVVL KLNGGLGTTM 100
    GCTGPKSVIE VRNGLTFLDL IVKQIEALNA KFGCSVPLLL MNSFNTHDDT 150
    LKIVEKYANS NIDIHTFNQS QYPRLVTEDF APLPCKGNSG KDGWYPPGHG 200
    DVFPSLMNSG KLDALLAKGK EYVFVANSDN LGAIVDLKIL NHLILNKNEY 250
    CMEVTPKTLA DVKGGTLISY EGKVQLLEIA QVPDEHVNEF KSIEKFKIFN 300
    TNNLWVNLSA IKRLVEADAL KMEIIPNPKE VDGVKVLQLE TAAGAAIKFF 350
    DRAIGANVPR SRFLPVKATS DLLLVQSDLY TLTDEGYVIR NPARSNPSNP 400
    SIELGPEFKK VANFLGRFKS IPSIIDLDSL KVTGDVWFGS GVTLKGKVTV 450
    AAKSGVKLEI PDGAVIANKD INGPEDI 477
    Length:477
    Mass (Da):51,874
    Last modified:January 23, 2007 - v3
    Checksum:i060E8D08AAE22709
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21A → V in AAB71613. (PubMed:9074509)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti5 – 51T → A in strain: cv. Desiree, cv. ND860-2 and cv. Russet Burbank-1.
    Natural varianti30 – 301E → D in strain: cv. Desiree, cv. ND860-2 and cv. Russet Burbank-1.
    Natural varianti82 – 821K → N in strain: cv. Desiree, cv. ND860-2 and cv. Russet Burbank-1.
    Natural varianti445 – 4451K → E in strain: cv. Desiree, cv. ND860-2 and cv. Russet Burbank-1.
    Natural varianti450 – 4501V → I in strain: cv. Desiree, cv. ND860-2 and cv. Russet Burbank-1.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D00667 mRNA. Translation: BAA00570.1.
    U20345 Genomic DNA. Translation: AAB71613.1.
    Z18924 mRNA. Translation: CAA79357.1.
    AY082618 mRNA. Translation: AAL99193.1.
    AY082619 mRNA. Translation: AAL99194.1.
    PIRiJX0128. XNPOU.
    S31431.
    UniGeneiStu.331.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D00667 mRNA. Translation: BAA00570.1 .
    U20345 Genomic DNA. Translation: AAB71613.1 .
    Z18924 mRNA. Translation: CAA79357.1 .
    AY082618 mRNA. Translation: AAL99193.1 .
    AY082619 mRNA. Translation: AAL99194.1 .
    PIRi JX0128. XNPOU.
    S31431.
    UniGenei Stu.331.

    3D structure databases

    ProteinModelPortali P19595.
    SMRi P19595. Positions 15-477.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P19595.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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. "UDP-glucose pyrophosphorylase from potato tuber: cDNA cloning and sequencing."
      Katsube T., Kazuta Y., Mori H., Nakano K., Tanizawa K., Fukui T.
      J. Biochem. 108:321-326(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], ACETYLATION AT ALA-2.
      Tissue: Tuber.
    2. "Organization and transcription of the gene encoding potato UDP-glucose pyrophosphorylase."
      Borovkov A.Y., McClean P.E., Secor G.A.
      Gene 186:293-297(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: cv. Lemhi Russet.
    3. "UDP-glucose pyrophosphorylase of potato tuber: cDNA sequence, transgenic tuber-specific inhibition and control of post-harvest sugar metabolism."
      Spychalla J.P., Bevan M.W.
      Submitted (DEC-1992) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. Desiree.
      Tissue: Tuber.
    4. "Molecular cloning and sequence variation of UDP-glucose pyrophosphorylase cDNAs from potatoes sensitive and resistant to cold sweetening."
      Sowokinos J.R., Vigdorovich V., Abrahamsen M.
      J. Plant Physiol. 161:947-955(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. ND860-2 and cv. Russet Burbank-1.
    5. "UDP-glucose pyrophosphorylase from potato tuber: purification and characterization."
      Nakano K., Omura Y., Tagaya M., Fukui T.
      J. Biochem. 106:528-532(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION.
      Tissue: Tuber.
    6. "Expression in Escherichia coli of UDP-glucose pyrophosphorylase cDNA from potato tuber and functional assessment of the five lysyl residues located at the substrate-binding site."
      Katsube T., Kazuta Y., Tanizawa K., Fukui T.
      Biochemistry 30:8546-8551(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF LYSINE RESIDUES.

    Entry informationi

    Entry nameiUGPA_SOLTU
    AccessioniPrimary (citable) accession number: P19595
    Secondary accession number(s): Q43192, Q5F1U8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 85 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3