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P09148

- GAL7_ECOLI

UniProt

P09148 - GAL7_ECOLI

Protein

Galactose-1-phosphate uridylyltransferase

Gene

galT

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose.

    Cofactori

    Binds 1 iron ion per subunit.
    Binds 1 zinc ion per subunit.

    Kineticsi

    1. KM=0.200 mM for uridine 5'-diphosphate glucose1 Publication
    2. KM=0.303 mM for galactose-1-phosphate1 Publication
    3. KM=0.121 mM for uridine 5'-diphosphate galactose1 Publication
    4. KM=0.157 mM for glucose-1-phosphate1 Publication

    Vmax=180 µmol/min/mg enzyme1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi52 – 521Zinc
    Metal bindingi55 – 551Zinc
    Metal bindingi115 – 1151Zinc
    Metal bindingi164 – 1641Zinc
    Active sitei166 – 1661Tele-UMP-histidine intermediate1 PublicationPROSITE-ProRule annotation
    Metal bindingi182 – 1821Iron
    Metal bindingi281 – 2811Iron
    Metal bindingi296 – 2961Iron
    Metal bindingi298 – 2981Iron

    GO - Molecular functioni

    1. ferrous iron binding Source: EcoCyc
    2. galactokinase activity Source: CACAO
    3. UDP-glucose:hexose-1-phosphate uridylyltransferase activity Source: EcoCyc
    4. zinc ion binding Source: EcoCyc

    GO - Biological processi

    1. carbohydrate phosphorylation Source: GOC
    2. galactose catabolic process via UDP-galactose Source: EcoCyc

    Keywords - Molecular functioni

    Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    Carbohydrate metabolism, Galactose metabolism

    Keywords - Ligandi

    Iron, Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciEcoCyc:GALACTURIDYLYLTRANS-MONOMER.
    ECOL316407:JW0741-MONOMER.
    MetaCyc:GALACTURIDYLYLTRANS-MONOMER.
    BRENDAi2.7.7.12. 2026.
    SABIO-RKP09148.
    UniPathwayiUPA00214.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Galactose-1-phosphate uridylyltransferase (EC:2.7.7.12)
    Short name:
    Gal-1-P uridylyltransferase
    Alternative name(s):
    UDP-glucose--hexose-1-phosphate uridylyltransferase
    Gene namesi
    Name:galT
    Synonyms:galB
    Ordered Locus Names:b0758, JW0741
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10366. galT.

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi160 – 1601C → S or A: Slight inhibition of enzymatic activity. 1 Publication
    Mutagenesisi161 – 1611S → A: 7000-fold reduction in specific activity. 1 Publication
    Mutagenesisi166 – 1661H → G: Abolishes enzymatic activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 348348Galactose-1-phosphate uridylyltransferasePRO_0000169894Add
    BLAST

    Proteomic databases

    PaxDbiP09148.
    PRIDEiP09148.

    Expressioni

    Gene expression databases

    GenevestigatoriP09148.

    Interactioni

    Subunit structurei

    Homodimer.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    nadEP188431EBI-1120083,EBI-548960

    Protein-protein interaction databases

    DIPiDIP-9735N.
    IntActiP09148. 1 interaction.
    STRINGi511145.b0758.

    Structurei

    Secondary structure

    1
    348
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni6 – 83
    Beta strandi11 – 144
    Turni16 – 183
    Beta strandi21 – 244
    Helixi28 – 303
    Beta strandi73 – 764
    Beta strandi95 – 973
    Beta strandi99 – 1013
    Beta strandi104 – 1118
    Helixi119 – 1213
    Helixi124 – 14421
    Beta strandi146 – 15510
    Helixi156 – 1583
    Beta strandi164 – 17411
    Helixi177 – 19317
    Helixi197 – 20812
    Beta strandi212 – 2154
    Beta strandi217 – 2226
    Beta strandi233 – 2397
    Helixi244 – 2463
    Helixi249 – 27022
    Beta strandi276 – 2816
    Beta strandi285 – 2884
    Beta strandi296 – 3005
    Beta strandi305 – 3084
    Helixi316 – 3194
    Beta strandi323 – 3264
    Helixi328 – 3369
    Helixi343 – 3464

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GUPX-ray1.80A/B/C/D1-348[»]
    1GUQX-ray1.80A/B/C/D1-348[»]
    1HXPX-ray1.80A/B1-348[»]
    1HXQX-ray1.86A/B1-348[»]
    ProteinModelPortaliP09148.
    SMRiP09148. Positions 2-348.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP09148.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1085.
    HOGENOMiHOG000230490.
    KOiK00965.
    OMAiEHPHRRF.
    OrthoDBiEOG6CCH5M.
    PhylomeDBiP09148.

    Family and domain databases

    Gene3Di3.30.428.10. 2 hits.
    InterProiIPR001937. GalP_UDPtransf1.
    IPR019779. GalP_UDPtransf1_His-AS.
    IPR005850. GalP_Utransf_C.
    IPR005849. GalP_Utransf_N.
    IPR011146. HIT-like.
    [Graphical view]
    PANTHERiPTHR11943. PTHR11943. 1 hit.
    PfamiPF02744. GalP_UDP_tr_C. 1 hit.
    PF01087. GalP_UDP_transf. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000808. GalT. 1 hit.
    SUPFAMiSSF54197. SSF54197. 2 hits.
    TIGRFAMsiTIGR00209. galT_1. 1 hit.
    PROSITEiPS00117. GAL_P_UDP_TRANSF_I. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P09148-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTQFNPVDHP HRRYNPLTGQ WILVSPHRAK RPWQGAQETP AKQVLPAHDP    50
    DCFLCAGNVR VTGDKNPDYT GTYVFTNDFA ALMSDTPDAP ESHDPLMRCQ 100
    SARGTSRVIC FSPDHSKTLP ELSVAALTEI VKTWQEQTAE LGKTYPWVQV 150
    FENKGAAMGC SNPHPHGQIW ANSFLPNEAE REDRLQKEYF AEQKSPMLVD 200
    YVQRELADGS RTVVETEHWL AVVPYWAAWP FETLLLPKAH VLRITDLTDA 250
    QRSDLALALK KLTSRYDNLF QCSFPYSMGW HGAPFNGEEN QHWQLHAHFY 300
    PPLLRSATVR KFMVGYEMLA ETQRDLTAEQ AAERLRAVSD IHFRESGV 348
    Length:348
    Mass (Da):39,646
    Last modified:November 1, 1997 - v2
    Checksum:i3D55D2CB38D8C9A2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti29 – 313AKR → LS in CAA29574. (PubMed:3022232)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X06226 Genomic DNA. Translation: CAA29574.1.
    U00096 Genomic DNA. Translation: AAC73845.1.
    AP009048 Genomic DNA. Translation: BAA35420.1.
    X02306 Genomic DNA. Translation: CAA26171.1.
    PIRiS00722. XNECUD.
    RefSeqiNP_415279.1. NC_000913.3.
    YP_489031.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73845; AAC73845; b0758.
    BAA35420; BAA35420; BAA35420.
    GeneIDi12932709.
    945357.
    KEGGiecj:Y75_p0731.
    eco:b0758.
    PATRICi32116717. VBIEscCol129921_0784.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X06226 Genomic DNA. Translation: CAA29574.1 .
    U00096 Genomic DNA. Translation: AAC73845.1 .
    AP009048 Genomic DNA. Translation: BAA35420.1 .
    X02306 Genomic DNA. Translation: CAA26171.1 .
    PIRi S00722. XNECUD.
    RefSeqi NP_415279.1. NC_000913.3.
    YP_489031.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GUP X-ray 1.80 A/B/C/D 1-348 [» ]
    1GUQ X-ray 1.80 A/B/C/D 1-348 [» ]
    1HXP X-ray 1.80 A/B 1-348 [» ]
    1HXQ X-ray 1.86 A/B 1-348 [» ]
    ProteinModelPortali P09148.
    SMRi P09148. Positions 2-348.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-9735N.
    IntActi P09148. 1 interaction.
    STRINGi 511145.b0758.

    Proteomic databases

    PaxDbi P09148.
    PRIDEi P09148.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC73845 ; AAC73845 ; b0758 .
    BAA35420 ; BAA35420 ; BAA35420 .
    GeneIDi 12932709.
    945357.
    KEGGi ecj:Y75_p0731.
    eco:b0758.
    PATRICi 32116717. VBIEscCol129921_0784.

    Organism-specific databases

    EchoBASEi EB0361.
    EcoGenei EG10366. galT.

    Phylogenomic databases

    eggNOGi COG1085.
    HOGENOMi HOG000230490.
    KOi K00965.
    OMAi EHPHRRF.
    OrthoDBi EOG6CCH5M.
    PhylomeDBi P09148.

    Enzyme and pathway databases

    UniPathwayi UPA00214 .
    BioCyci EcoCyc:GALACTURIDYLYLTRANS-MONOMER.
    ECOL316407:JW0741-MONOMER.
    MetaCyc:GALACTURIDYLYLTRANS-MONOMER.
    BRENDAi 2.7.7.12. 2026.
    SABIO-RK P09148.

    Miscellaneous databases

    EvolutionaryTracei P09148.
    PROi P09148.

    Gene expression databases

    Genevestigatori P09148.

    Family and domain databases

    Gene3Di 3.30.428.10. 2 hits.
    InterProi IPR001937. GalP_UDPtransf1.
    IPR019779. GalP_UDPtransf1_His-AS.
    IPR005850. GalP_Utransf_C.
    IPR005849. GalP_Utransf_N.
    IPR011146. HIT-like.
    [Graphical view ]
    PANTHERi PTHR11943. PTHR11943. 1 hit.
    Pfami PF02744. GalP_UDP_tr_C. 1 hit.
    PF01087. GalP_UDP_transf. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000808. GalT. 1 hit.
    SUPFAMi SSF54197. SSF54197. 2 hits.
    TIGRFAMsi TIGR00209. galT_1. 1 hit.
    PROSITEi PS00117. GAL_P_UDP_TRANSF_I. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequences of the gal E gene and the gal T gene of E. coli."
      Lemaire H.-G., Mueller-Hill B.
      Nucleic Acids Res. 14:7705-7711(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "Structure of the galactokinase gene of Escherichia coli, the last (?) gene of the gal operon."
      Debouck C., Riccio A., Schumperli D., McKenney K., Jeffers J., Hughes C., Rosenberg M., Heusterspreute M., Brunel F., Davison J.
      Nucleic Acids Res. 13:1841-1853(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 294-348.
    6. "The nucleotide sequence of the gal T gene of Escherichia coli."
      Cornwell T.L., Adhya S.L., Reznikoff W.S., Frey P.A.
      Nucleic Acids Res. 15:8116-8116(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 27-38.
    7. "Galactose-1-phosphate uridylyltransferase: isolation and properties of a uridylyl-enzyme intermediate."
      Wong L.J., Sheu K.F., Lee S.L., Frey P.A.
      Biochemistry 16:1010-1016(1977) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    8. "The structure of nucleotidylated histidine-166 of galactose-1-phosphate uridylyltransferase provides insight into phosphoryl group transfer."
      Wedekind J.E., Frey P.A., Rayment I.
      Biochemistry 35:11560-11569(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVE SITE HIS-166.
    9. "Roles of two conserved amino acid residues in the active site of galactose-1-phosphate uridylyltransferase: an essential serine and a nonessential cysteine."
      Geeganage S., Ling V.W., Frey P.A.
      Biochemistry 39:5397-5404(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: KINETIC PARAMETERS, MUTAGENESIS OF CYS-160 AND SER-161.
    10. "Three-dimensional structure of galactose-1-phosphate uridylyltransferase from Escherichia coli at 1.8-A resolution."
      Wedekind J.E., Frey P.A., Rayment I.
      Biochemistry 34:11049-11061(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
    11. "Structural analysis of the H166G site-directed mutant of galactose-1-phosphate uridylyltransferase complexed with either UDP-glucose or UDP-galactose: detailed description of the nucleotide sugar binding site."
      Thoden J.B., Ruzicka F.J., Frey P.A., Rayment I., Holden H.M.
      Biochemistry 36:1212-1222(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), MUTAGENESIS OF HIS-166.

    Entry informationi

    Entry nameiGAL7_ECOLI
    AccessioniPrimary (citable) accession number: P09148
    Secondary accession number(s): P78270
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 136 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3