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P19595 (UGPA_SOLTU) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
UTP--glucose-1-phosphate uridylyltransferase

EC=2.7.7.9
Alternative name(s):
UDP-glucose pyrophosphorylase
Short name=UDPGP
Short name=UGPase
OrganismSolanum tuberosum (Potato) [Reference proteome]
Taxonomic identifier4113 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanum

Protein attributes

Sequence length477 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

Magnesium.

Enzyme regulation

Inhibition by uncomplexed, free UTP.

Subunit structure

Monomer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the UDPGP type 1 family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMagnesium
   Molecular functionNucleotidyltransferase
Transferase
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcallose deposition in cell wall

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

cellular response to phosphate starvation

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

pollen development

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

response to cadmium ion

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

response to salt stress

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

   Cellular_componentcytosol

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

plasma membrane

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

pollen tube

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

   Molecular_functionUTP:glucose-1-phosphate uridylyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 477476UTP--glucose-1-phosphate uridylyltransferase
PRO_0000185762

Amino acid modifications

Modified residue21N-acetylalanine Ref.1

Natural variations

Natural variant51T → A in strain: cv. Desiree, cv. ND860-2 and cv. Russet Burbank-1.
Natural variant301E → D in strain: cv. Desiree, cv. ND860-2 and cv. Russet Burbank-1.
Natural variant821K → N in strain: cv. Desiree, cv. ND860-2 and cv. Russet Burbank-1.
Natural variant4451K → E in strain: cv. Desiree, cv. ND860-2 and cv. Russet Burbank-1.
Natural variant4501V → I in strain: cv. Desiree, cv. ND860-2 and cv. Russet Burbank-1.

Experimental info

Mutagenesis2631K → Q: Significant decreased Vmax values. Ref.6
Mutagenesis3291K → Q: Increased Km, Vmax like wild-type. Ref.6
Mutagenesis3671K → Q: Almost complete loss of activity. Ref.6
Mutagenesis4091K → Q: Activity almost like wild-type. Ref.6
Mutagenesis4101K → Q: Activity almost like wild-type. Ref.6
Sequence conflict21A → V in AAB71613. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P19595 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 060E8D08AAE22709

FASTA47751,874
        10         20         30         40         50         60 
MATATTLSPA DAEKLNNLKS AVAGLNQISE NEKSGFINLV GRYLSGEAQH IDWSKIQTPT 

        70         80         90        100        110        120 
DEVVVPYDKL APLSEDPAET KKLLDKLVVL KLNGGLGTTM GCTGPKSVIE VRNGLTFLDL 

       130        140        150        160        170        180 
IVKQIEALNA KFGCSVPLLL MNSFNTHDDT LKIVEKYANS NIDIHTFNQS QYPRLVTEDF 

       190        200        210        220        230        240 
APLPCKGNSG KDGWYPPGHG DVFPSLMNSG KLDALLAKGK EYVFVANSDN LGAIVDLKIL 

       250        260        270        280        290        300 
NHLILNKNEY CMEVTPKTLA DVKGGTLISY EGKVQLLEIA QVPDEHVNEF KSIEKFKIFN 

       310        320        330        340        350        360 
TNNLWVNLSA IKRLVEADAL KMEIIPNPKE VDGVKVLQLE TAAGAAIKFF DRAIGANVPR 

       370        380        390        400        410        420 
SRFLPVKATS DLLLVQSDLY TLTDEGYVIR NPARSNPSNP SIELGPEFKK VANFLGRFKS 

       430        440        450        460        470 
IPSIIDLDSL KVTGDVWFGS GVTLKGKVTV AAKSGVKLEI PDGAVIANKD INGPEDI 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRXNPOU. JX0128.
S31431.
UniGeneStu.331.

3D structure databases

ProteinModelPortalP19595.
SMRP19595. Positions 15-477.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP19595.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR002618. UDPGP_trans.
IPR016267. UDPGP_trans_subgr.
[Graphical view]
PANTHERPTHR11952. PTHR11952. 1 hit.
PTHR11952:SF1. PTHR11952:SF1. 1 hit.
PfamPF01704. UDPGP. 1 hit.
[Graphical view]
PIRSFPIRSF000806. UDPGP. 1 hit.
ProtoNetSearch...

Entry information

Entry nameUGPA_SOLTU
AccessionPrimary (citable) accession number: P19595
Secondary accession number(s): Q43192, Q5F1U8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: January 23, 2007
Last modified: March 19, 2014
This is version 82 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families