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P19595

- UGPA_SOLTU

UniProt

P19595 - UGPA_SOLTU

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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

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
Complete GO annotation...

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
Complete GO annotation...

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 – 11Removed
Chaini2 – 477476UTP--glucose-1-phosphate uridylyltransferase
PRO_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.

Family & Domainsi

Sequence similaritiesi

Belongs to the UDPGP type 1 family.

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

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21A → V in AAB71613. 1 Publication

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: September 3, 2014
This is version 84 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

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