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Reviewed, UniProtKB/Swiss-Prot P09148 (GAL7_ECOLI)

Last modified June 16, 2009. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length348 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

UDP-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose 1-phosphate + UDP-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
P09148-1 [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: 3022232] [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: 8905232] [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 277:1453-1474(1997) [PubMed: 9278503] [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: 16738553] [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: 3158881] [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: 2823224] [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: 321007] [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: 8794735] [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: 10820011] [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: 7669762] [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: 9063869] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), MUTAGENESIS OF HIS-166.

Cross-references

Sequence databases

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.
RefSeqAP_001389.1.
NP_415279.1.

3D structure databases

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[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:9735N.
IntActP09148. 1 interaction.

Genome annotation databases

GeneID945357.
GenomeReviewsGene locus JW0741 in contig AP009048_GR.
Gene locus b0758 in contig U00096_GR.
KEGGecj:JW0741.
eco:b0758.

Organism-specific databases

EchoBASEEB0361.
EcoGeneEG10366. galT.
CMRSearch...

Phylogenomic databases

HOGENOMP09148.
OMAP09148. DHWQLHA.

Enzyme and pathway databases

BioCycEcoCyc:GALACTURIDYLYLTRANS-MON.
MetaCyc:GALACTURIDYLYLTRANS-MON.
BRENDA2.7.7.12. 246.

Family and domain databases

InterProIPR001937. GalP_UDPtransf1.
IPR019779. GalP_UDPtransf1_His-AS.
IPR005850. GalP_Utransf_C.
IPR005849. GalP_Utransf_N.
IPR011151. His_triad_motif.
[Graphical view]
Gene3DG3DSA:3.30.428.10. His_triad_motif. 2 hits.
PANTHERPTHR11943. GalP_UDPtransf1. 1 hit.
PfamPF02744. GalP_UDP_tr_C. 1 hit.
PF01087. GalP_UDP_transf. 1 hit.
[Graphical view]
PIRSFPIRSF000808. GalT. 1 hit.
ProDomPD005051. GalP_Utransf. 2 hits.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00209. galT_1. 1 hit.
PROSITEPS00117. GAL_P_UDP_TRANSF_I. 1 hit.
[Graphical view]
ProtoNetSearch...

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: June 16, 2009
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Escherichia coli

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents