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Protein

Galactose-1-phosphate uridylyltransferase

Gene

galT

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • Fe cationNote: Binds 1 Fe cation per subunit.
  • Zn2+Note: 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
  1. Vmax=180 µmol/min/mg enzyme1 Publication

Pathway:igalactose metabolism

This protein is involved in the pathway galactose metabolism, which is part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the pathway galactose metabolism and in Carbohydrate metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi52 – 521Zinc
Metal bindingi55 – 551Zinc
Metal bindingi115 – 1151Zinc
Metal bindingi164 – 1641Zinc
Active sitei166 – 1661Tele-UMP-histidine intermediatePROSITE-ProRule annotation1 Publication
Metal bindingi182 – 1821Iron
Metal bindingi281 – 2811Iron
Metal bindingi296 – 2961Iron
Metal bindingi298 – 2981Iron

GO - Molecular functioni

  • ferrous iron binding Source: EcoCyc
  • galactokinase activity Source: CACAO
  • UDP-glucose:hexose-1-phosphate uridylyltransferase activity Source: EcoCyc
  • zinc ion binding Source: EcoCyc

GO - Biological processi

  • carbohydrate phosphorylation Source: GOC
  • galactose catabolic process via UDP-galactose Source: EcoCyc
Complete GO annotation...

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 Componenti: Chromosome UP000000625 Componenti: 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.

Interactioni

Subunit structurei

Homodimer.

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 – 83Combined sources
Beta strandi11 – 144Combined sources
Turni16 – 183Combined sources
Beta strandi21 – 244Combined sources
Helixi28 – 303Combined sources
Beta strandi73 – 764Combined sources
Beta strandi95 – 973Combined sources
Beta strandi99 – 1013Combined sources
Beta strandi104 – 1118Combined sources
Helixi119 – 1213Combined sources
Helixi124 – 14421Combined sources
Beta strandi146 – 15510Combined sources
Helixi156 – 1583Combined sources
Beta strandi164 – 17411Combined sources
Helixi177 – 19317Combined sources
Helixi197 – 20812Combined sources
Beta strandi212 – 2154Combined sources
Beta strandi217 – 2226Combined sources
Beta strandi233 – 2397Combined sources
Helixi244 – 2463Combined sources
Helixi249 – 27022Combined sources
Beta strandi276 – 2816Combined sources
Beta strandi285 – 2884Combined sources
Beta strandi296 – 3005Combined sources
Beta strandi305 – 3084Combined sources
Helixi316 – 3194Combined sources
Beta strandi323 – 3264Combined sources
Helixi328 – 3369Combined sources
Helixi343 – 3464Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP09148.
KOiK00965.
OMAiWHYAPFF.
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

        10         20         30         40         50
MTQFNPVDHP HRRYNPLTGQ WILVSPHRAK RPWQGAQETP AKQVLPAHDP
60 70 80 90 100
DCFLCAGNVR VTGDKNPDYT GTYVFTNDFA ALMSDTPDAP ESHDPLMRCQ
110 120 130 140 150
SARGTSRVIC FSPDHSKTLP ELSVAALTEI VKTWQEQTAE LGKTYPWVQV
160 170 180 190 200
FENKGAAMGC SNPHPHGQIW ANSFLPNEAE REDRLQKEYF AEQKSPMLVD
210 220 230 240 250
YVQRELADGS RTVVETEHWL AVVPYWAAWP FETLLLPKAH VLRITDLTDA
260 270 280 290 300
QRSDLALALK KLTSRYDNLF QCSFPYSMGW HGAPFNGEEN QHWQLHAHFY
310 320 330 340
PPLLRSATVR KFMVGYEMLA ETQRDLTAEQ AAERLRAVSD IHFRESGV
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:
EMBLi
GenBanki
DDBJi
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.
WP_000191497.1. NZ_CP010445.1.

Genome annotation databases

EnsemblBacteriaiAAC73845; AAC73845; b0758.
BAA35420; BAA35420; BAA35420.
GeneIDi945357.
KEGGieco:b0758.
PATRICi32116717. VBIEscCol129921_0784.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
WP_000191497.1. NZ_CP010445.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

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

Proteomic databases

PaxDbiP09148.
PRIDEiP09148.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73845; AAC73845; b0758.
BAA35420; BAA35420; BAA35420.
GeneIDi945357.
KEGGieco:b0758.
PATRICi32116717. VBIEscCol129921_0784.

Organism-specific databases

EchoBASEiEB0361.
EcoGeneiEG10366. galT.

Phylogenomic databases

eggNOGiCOG1085.
HOGENOMiHOG000230490.
InParanoidiP09148.
KOiK00965.
OMAiWHYAPFF.
OrthoDBiEOG6CCH5M.
PhylomeDBiP09148.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP09148.
PROiP09148.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: July 22, 2015
This is version 145 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

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.