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P09148 (GAL7_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Galactose-1-phosphate uridylyltransferase

Short name=Gal-1-P uridylyltransferase
EC=2.7.7.12
Alternative name(s):
UDP-glucose--hexose-1-phosphate uridylyltransferase
Gene names
Name:galT
Synonyms:galB
Ordered Locus Names:b0758, JW0741
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length348 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 1 iron ion per subunit.

Binds 1 zinc ion per subunit.

Pathway

Carbohydrate metabolism; galactose metabolism.

Subunit structure

Homodimer.

Sequence similarities

Belongs to the galactose-1-phosphate uridylyltransferase type 1 family.

Biophysicochemical properties

Kinetic parameters:

KM=0.200 mM for uridine 5'-diphosphate glucose Ref.9

KM=0.303 mM for galactose-1-phosphate

KM=0.121 mM for uridine 5'-diphosphate galactose

KM=0.157 mM for glucose-1-phosphate

Vmax=180 µmol/min/mg enzyme

Binary interactions

With

Entry

#Exp.

IntAct

Notes

nadEP188431EBI-1120083,EBI-548960

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 348348Galactose-1-phosphate uridylyltransferase
PRO_0000169894

Sites

Active site1661Tele-UMP-histidine intermediate Ref.8
Metal binding521Zinc
Metal binding551Zinc
Metal binding1151Zinc
Metal binding1641Zinc
Metal binding1821Iron
Metal binding2811Iron
Metal binding2961Iron
Metal binding2981Iron

Experimental info

Mutagenesis1601C → S or A: Slight inhibition of enzymatic activity. Ref.9
Mutagenesis1611S → A: 7000-fold reduction in specific activity. Ref.9
Mutagenesis1661H → G: Abolishes enzymatic activity. Ref.11
Sequence conflict29 – 313AKR → LS in CAA29574. Ref.1

Secondary structure

.......................................................... 348
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P09148 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 3D55D2CB38D8C9A2

FASTA34839,646
        10         20         30         40         50         60 
MTQFNPVDHP HRRYNPLTGQ WILVSPHRAK RPWQGAQETP AKQVLPAHDP DCFLCAGNVR 

        70         80         90        100        110        120 
VTGDKNPDYT GTYVFTNDFA ALMSDTPDAP ESHDPLMRCQ SARGTSRVIC FSPDHSKTLP 

       130        140        150        160        170        180 
ELSVAALTEI VKTWQEQTAE LGKTYPWVQV FENKGAAMGC SNPHPHGQIW ANSFLPNEAE 

       190        200        210        220        230        240 
REDRLQKEYF AEQKSPMLVD YVQRELADGS RTVVETEHWL AVVPYWAAWP FETLLLPKAH 

       250        260        270        280        290        300 
VLRITDLTDA QRSDLALALK KLTSRYDNLF QCSFPYSMGW HGAPFNGEEN QHWQLHAHFY 

       310        320        330        340 
PPLLRSATVR KFMVGYEMLA ETQRDLTAEQ AAERLRAVSD IHFRESGV 

« Hide

References

« Hide 'large scale' references
[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]"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."
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. expand/collapse author list , 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.
DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
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.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X06226 Genomic DNA. Translation: CAA29574.1.
U00096 Genomic DNA. Translation: AAC73845.1.
AP009048 Genomic DNA. Translation: BAA35420.1.
X02306 Genomic DNA. Translation: CAA26171.1.
PIRXNECUD. S00722.
RefSeqNP_415279.1. NC_000913.3.
YP_489031.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP09148.
SMRP09148. Positions 2-348.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-9735N.
IntActP09148. 1 interaction.
STRING511145.b0758.

Proteomic databases

PaxDbP09148.
PRIDEP09148.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73845; AAC73845; b0758.
BAA35420; BAA35420; BAA35420.
GeneID12932709.
945357.
KEGGecj:Y75_p0731.
eco:b0758.
PATRIC32116717. VBIEscCol129921_0784.

Organism-specific databases

EchoBASEEB0361.
EcoGeneEG10366. galT.

Phylogenomic databases

eggNOGCOG1085.
HOGENOMHOG000230490.
KOK00965.
OMAEHPHRRF.
OrthoDBEOG6CCH5M.
PhylomeDBP09148.

Enzyme and pathway databases

BioCycEcoCyc:GALACTURIDYLYLTRANS-MONOMER.
ECOL316407:JW0741-MONOMER.
MetaCyc:GALACTURIDYLYLTRANS-MONOMER.
BRENDA2.7.7.12. 2026.
SABIO-RKP09148.
UniPathwayUPA00214.

Gene expression databases

GenevestigatorP09148.

Family and domain databases

Gene3D3.30.428.10. 2 hits.
InterProIPR001937. GalP_UDPtransf1.
IPR019779. GalP_UDPtransf1_His-AS.
IPR005850. GalP_Utransf_C.
IPR005849. GalP_Utransf_N.
IPR011146. HIT-like.
[Graphical view]
PANTHERPTHR11943. PTHR11943. 1 hit.
PfamPF02744. GalP_UDP_tr_C. 1 hit.
PF01087. GalP_UDP_transf. 1 hit.
[Graphical view]
PIRSFPIRSF000808. GalT. 1 hit.
SUPFAMSSF54197. SSF54197. 2 hits.
TIGRFAMsTIGR00209. galT_1. 1 hit.
PROSITEPS00117. GAL_P_UDP_TRANSF_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP09148.
PROP09148.

Entry information

Entry nameGAL7_ECOLI
AccessionPrimary (citable) accession number: P09148
Secondary accession number(s): P78270
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 1, 1997
Last modified: May 14, 2014
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene