Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

UTP--glucose-1-phosphate uridylyltransferase

Gene
N/A
Organism
Solanum tuberosum (Potato)
Status
Reviewed-Annotation score: 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

Enzyme regulationi

Inhibition by uncomplexed, free UTP.

GO - Molecular functioni

GO - Biological processi

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 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

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 – 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

« Hide

        10         20         30         40         50
MATATTLSPA DAEKLNNLKS AVAGLNQISE NEKSGFINLV GRYLSGEAQH
60 70 80 90 100
IDWSKIQTPT DEVVVPYDKL APLSEDPAET KKLLDKLVVL KLNGGLGTTM
110 120 130 140 150
GCTGPKSVIE VRNGLTFLDL IVKQIEALNA KFGCSVPLLL MNSFNTHDDT
160 170 180 190 200
LKIVEKYANS NIDIHTFNQS QYPRLVTEDF APLPCKGNSG KDGWYPPGHG
210 220 230 240 250
DVFPSLMNSG KLDALLAKGK EYVFVANSDN LGAIVDLKIL NHLILNKNEY
260 270 280 290 300
CMEVTPKTLA DVKGGTLISY EGKVQLLEIA QVPDEHVNEF KSIEKFKIFN
310 320 330 340 350
TNNLWVNLSA IKRLVEADAL KMEIIPNPKE VDGVKVLQLE TAAGAAIKFF
360 370 380 390 400
DRAIGANVPR SRFLPVKATS DLLLVQSDLY TLTDEGYVIR NPARSNPSNP
410 420 430 440 450
SIELGPEFKK VANFLGRFKS IPSIIDLDSL KVTGDVWFGS GVTLKGKVTV
460 470
AAKSGVKLEI PDGAVIANKD INGPEDI
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Proteomic databases

PRIDEiP19595.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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.
ProtoNetiSearch...

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: January 7, 2015
This is version 88 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.