Entry Information
Protein Name GalU
Accession No P0AEP3
Protein description UTP-glucose-1-phosphate uridylyltransferase
pI/Mw (Da)
Theoretical Experimental
5.11/32811.07 -
Protein function and expression May play a role in stationary phase survival.
Reference(s) Lopez-Campistrous, A., P. Semchuk, L. Burke, T. Palmer-Stone, S. J. Brokx, G. Broderick, D. Bottorff, S. Bolch, J. H. Weiner, and M. J. Ellison. 2005. Localization, annotation & comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell. Proteomics 4:1205-1209. (NCBI)

Swiss-Prot Database Reference

Entry information
Entry Name GALU_ECOLI
Primary accession number P0AEP3
Secondary accession numbers P25520 
Integrated into Swiss-Prot on 2005-12-20
Sequence was last modified on 2005-12-20 (Sequence version 1)
Annotations were last modified on 2006-05-30 (Entry version 7)
Name and origin of the protein
Protein name UTP--glucose-1-phosphate uridylyltransferase
Synonyms EC 2.7.7.9 UTP--glucose-1-phosphate uridylyltransferase
UDP-glucose pyrophosphorylase
UDPGP
Alpha-D-glucosyl-1-phosphate uridylyltransferase
Uridine diphosphoglucose pyrophosphorylase
Gene name Name : galU
OrderedLocusName : b1236
From Escherichia coli [TaxID:562] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia;
References
[1] NUCLEOTIDE SEQUENCE [GENOMIC DNA].
strain = K12
PubMed=1537791[NCBI, ExPASy, EBI, Israel, Japan]
Ueguchi C. , Ito K. ,
"Multicopy suppression: an approach to understanding intracellular functioning of the protein export system."
J. Bacteriol.174:1454-1461(1992) 
[2] NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10, AND CHARACTERIZATION.
strain = K12
PubMed=8169209[NCBI, ExPASy, EBI, Israel, Japan]
Weissborn A.C. , Liu Q. , Rumley M.K. , Kennedy E.P. ,
"UTP: alpha-D-glucose-1-phosphate uridylyltransferase of Escherichia coli: isolation and DNA sequence of the galU gene and purification of the enzyme."
J. Bacteriol.176:2611-2618(1994) 
[3] NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
strain = K12
PubMed=7961613[NCBI, ExPASy, EBI, Israel, Japan]
Hossain S.A. , Tanizawa K. , Kazuta Y. , Fukui T. ,
"Overproduction and characterization of recombinant UDP-glucose pyrophosphorylase from Escherichia coli K-12."
J. Biochem.115:965-972(1994) 
[4] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
strain = K12 / W3110 / ATCC 27325 / DSM 5911
DOI=10.1093/dnares/3.3.137;PubMed=8905232[NCBI, ExPASy, EBI, Israel, Japan]
Oshima T. , Aiba H. , Baba T. , Fujita K. , Hayashi K. , Honjo A. , Ikemoto K. , Inada T. , Itoh T. , Kajihara M. , Kanai K. , Kashimoto K. , Kimura S. , Kitagawa M. , Makino K. , Masuda S. , Miki T. , Mizobuchi K. , Mori H. , Motomura K. , Nakamura Y. , Nashimoto H. , Nishio Y. , Saito N. , Sampei G. , Seki Y. , Tagami H. , Takemoto K. , Wada C. , Yamamoto Y. , Yano M. , Horiuchi T. ,
"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map."
DNA Res.3:137-155(1996) 
[5] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
strain = K12 / MG1655 / ATCC 47076
DOI=10.1126/science.277.5331.1453;PubMed=9278503[NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R. , Plunkett G. III , Bloch C.A. , Perna N.T. , Burland V. , Riley M. , Collado-Vides J. , Glasner J.D. , Rode C.K. , Mayhew G.F. , Gregor J. , Davis N.W. , Kirkpatrick H.A. , Goeden M.A. , Rose D.J. , Mau B. , Shao Y. ,
"The complete genome sequence of Escherichia coli K-12."
Science277:1453-1474(1997) 
[6] PARTIAL PROTEIN SEQUENCE OF 1-17.
strain = K12 / EMG2
PubMed=9298646[NCBI, ExPASy, EBI, Israel, Japan]
Link A.J. , Robison K. , Church G.M. ,
"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
Electrophoresis18:1259-1313(1997) 
Comments
  • FUNCTION : May play a role in stationary phase survival
  • CATALYTIC ACTIVITY : UTP + alpha-D-glucose 1-phosphate = diphosphate + UDP-glucose
  • COFACTOR : Magnesium
  • SUBUNIT : Homotetramer or homopentamer
  • SIMILARITY : Belongs to the prokaryotic UDPGP family
  • Copyright
    Copyrighted by the UniProt Consortium, see http://www.uniprot.org/. Distributed under the Creative Commons Attribution-NoDerivs License.
    Cross-reference
    Sequence databases
    EMBL X59940;CAA42564.1;-;Genomic_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    M98830;AAA20118.1;-;Unassigned_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    AP009048;BAA36104.1;-;Genomic_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    U00096;AAC74318.1;-;Genomic_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    PIR G64870;JC2265.
    3D structure databases
    ModBase P0AEP3
    Protein-protein interaction databases
    DIP P0AEP3
    Enzyme and pathway databases
    BioCyc EcoCyc:GLUC1PURIDYLTRANS-MONOMER;-.
    2D gel databases
    SWISS-2DPAGE Get region on 2D PAGE
    Organism-specific gene databases
    EchoBASE EB1295;-.
    EcoGene EG11319;galU.
    HOGENOM [Family / Alignment / Tree]
    Family and domain databases
    InterPro IPR005771;GalU_trans_bac.
    IPR005835;NTP_transferase.
    Graphical view of domain structure
    Pfam PF00483;NTP_transferase;1.
    Pfam graphical view of domain structure
    TIGRFAMs TIGR01099;galU;1.
    BLOCKS P0AEP3
    Genome annotation databases
    GenomeReviews U00096_GR;b1236.
    Other
    ProtoNet P0AEP3
    UniRef View cluster of proteins with at least 50% / 90% / 100% identity
    Keyword
    Complete proteome; Direct protein sequencing; Kinase; Magnesium; Nucleotidyltransferase; Transferase;
    Features
    Feature table viewer Feature aligner
    Key  From   To Length  Description  FTId
    INIT_MET    0     0      
    CHAIN    1   301    301  UTP--glucose-1-phosphate uridylyltransferase  PRO_0000201354
    Sequence information
    Length: 301AA [This is the length of the unprocessed precursor] Molecular weight: 32811Da [This is the MW of the unprocessed precursor] CRC64: 29780B89857B16F7[This is a checksum on the sequence]
            10         20         30         40         50         60
    AAINTKVKKA VIPVAGLGTR MLPATKAIPK EMLPLVDKPL IQYVVNECIA AGITEIVLVT
            70         80         90        100        110        120
    HSSKNSIENH FDTSFELEAM LEKRVKRQLL DEVQSICPPH VTIMQVRQGL AKGLGHAVLC
           130        140        150        160        170        180
    AHPVVGDEPV AVILPDVILD EYESDLSQDN LAEMIRRFDE TGHSQIMVEP VADVTAYGVV
           190        200        210        220        230        240
    DCKGVELAPG ESVPMVGVVE KPKADVAPSN LAIVGRYVLS ADIWPLLAKT PPGAGDEIQL
           250        260        270        280        290        300
    TDAIDMLIEK ETVEAYHMKG KSHDCGNKLG YMQAFVEYGI RHNTLGTEFK AWLEEEMGIK
    
    K
    P0AEP3 in FASTA format