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UniProtKB/Swiss-Prot entry P09148


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name GAL7_ECOLI
Primary accession number P09148
Secondary accession number P78270
Integrated into Swiss-Prot on July 1, 1989
Sequence was last modified on November 1, 1997 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 91)
Name and origin of the protein
Protein name Galactose-1-phosphate uridylyltransferase
Synonyms Gal-1-P uridylyltransferase
EC 2.7.7.12
UDP-glucose--hexose-1-phosphate uridylyltransferase
Gene name
Name: galT
Synonyms: galB
OrderedLocusNames: b0758, JW0741
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1093/nar/14.19.7705; PubMed=3022232 [NCBI, ExPASy, EBI, Israel, Japan]
Lemaire H.-G., Mueller-Hill B.;
"Nucleotide sequences of the gal E gene and the gal T gene of E. coli.";
Nucleic Acids Res. 14:7705-7711(1986).
[2]
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).
[3]
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.";
Science 277:1453-1474(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 294-348.
DOI=10.1093/nar/13.6.1841; PubMed=3158881 [NCBI, ExPASy, EBI, Israel, Japan]
Debouck C., Riccio A., Schumperli D., McKenney K., Jeffers J., Hughes C., Rosenberg M., Heusterspreute M., Brunel F., Davison J.;
"Structure of the galactokinase gene of Escherichia coli, the last (?) gene of the gal operon.";
Nucleic Acids Res. 13:1841-1853(1985).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 27-38.
DOI=10.1093/nar/15.19.8116; PubMed=2823224 [NCBI, ExPASy, EBI, Israel, Japan]
Cornwell T.L., Adhya S.L., Reznikoff W.S., Frey P.A.;
"The nucleotide sequence of the gal T gene of Escherichia coli.";
Nucleic Acids Res. 15:8116-8116(1987).
[7]
CHARACTERIZATION.
DOI=10.1021/bi00624a032; PubMed=321007 [NCBI, ExPASy, EBI, Israel, Japan]
Wong L.J., Sheu K.F., Lee S.L., Frey P.A.;
"Galactose-1-phosphate uridylyltransferase: isolation and properties of a uridylyl-enzyme intermediate.";
Biochemistry 16:1010-1016(1977).
[8]
ACTIVE SITE HIS-166.
DOI=10.1021/bi9612677; PubMed=8794735 [NCBI, ExPASy, EBI, Israel, Japan]
Wedekind J.E., Frey P.A., Rayment I.;
"The structure of nucleotidylated histidine-166 of galactose-1-phosphate uridylyltransferase provides insight into phosphoryl group transfer.";
Biochemistry 35:11560-11569(1996).
[9]
KINETIC PARAMETERS, AND MUTAGENESIS OF CYS-160 AND SER-161.
DOI=10.1021/bi992594s; PubMed=10820011 [NCBI, ExPASy, EBI, Israel, Japan]
Geeganage S., Ling V.W., Frey P.A.;
"Roles of two conserved amino acid residues in the active site of galactose-1-phosphate uridylyltransferase: an essential serine and a nonessential cysteine.";
Biochemistry 39:5397-5404(2000).
[10]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
DOI=10.1021/bi00035a010; PubMed=7669762 [NCBI, ExPASy, EBI, Israel, Japan]
Wedekind J.E., Frey P.A., Rayment I.;
"Three-dimensional structure of galactose-1-phosphate uridylyltransferase from Escherichia coli at 1.8-A resolution.";
Biochemistry 34:11049-11061(1995).
[11]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), AND MUTAGENESIS OF HIS-166.
DOI=10.1021/bi9626517; PubMed=9063869 [NCBI, ExPASy, EBI, Israel, Japan]
Thoden J.B., Ruzicka F.J., Frey P.A., Rayment I., Holden H.M.;
"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.";
Biochemistry 36:1212-1222(1997).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X06226; CAA29574.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC73845.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA35420.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X02306; CAA26171.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S00722; XNECUD.
RefSeq AP_001389.1; -.
NP_415279.1; -.
3D structure databases
PDB
1GUP; X-ray; 1.80 A; A/B/C/D=1-348.[ExPASy / RCSB / EBI]
1GUQ; X-ray; 1.80 A; A/B/C/D=1-348.[ExPASy / RCSB / EBI]
1HXP; X-ray; 1.80 A; A/B=1-348.[ExPASy / RCSB / EBI]
1HXQ; X-ray; 1.86 A; A/B=1-348.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1GUP; -.
1GUQ; -.
1HXP; -.
1HXQ; -.
ModBase P09148.
Protein-protein interaction databases
DIP DIP:9735N; -.
IntAct P09148; -.
Enzyme and pathway databases
BioCyc EcoCyc:GALACTURIDYLYLTRANS-MON; -.
MetaCyc:GALACTURIDYLYLTRANS-MON; -.
Organism-specific databases
EchoBASE EB0361; -.
EcoGene EG10366; galT.
Ontologies
GO
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.
Family and domain databases
InterPro IPR001937; GalP_UDPtransf1.
IPR005850; GalP_Utransf_C.
IPR005849; GalP_Utransf_N.
IPR011151; His_triad_motif.
Graphical view of domain structure.
Gene3D G3DSA:3.30.428.10; His_triad_motif; 2.
PANTHER PTHR11943; GalP_UDPtransf1; 1.
Pfam PF02744; GalP_UDP_tr_C; 1.
PF01087; GalP_UDP_transf; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000808; GalT; 1.
ProDom PD005051; GalP_Utransf; 2.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR00209; galT_1; 1.
PROSITE PS00117; GAL_P_UDP_TRANSF_I; 1.
BLOCKS P09148.
Genome annotation databases
GeneID 945357; -.
GenomeReviews U00096_GR; b0758.
AP009048_GR; JW0741.
KEGG ecj:JW0741; -.
eco:b0758; -.
Phylogenomic databases
HOGENOM P09148; -.
Other
LinkHub P09148; -.
Genome annotation databases
CMR P09148; b0758.
Other
ProtoNet P09148.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Carbohydrate metabolism; Complete proteome; Galactose metabolism; Iron; Metal-binding; Nucleotidyltransferase; Transferase; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   348  348     Galactose-1-phosphate uridylyltransferase. PRO_0000169894
ACT_SITE   166   166        Tele-UMP-histidine intermediate. 
METAL   52    52        Zinc. 
METAL   55    55        Zinc. 
METAL   115   115        Zinc. 
METAL   164   164        Zinc. 
METAL   182   182        Iron. 
METAL   281   281        Iron. 
METAL   296   296        Iron. 
METAL   298   298        Iron. 
MUTAGEN   160   160        C->S,A: Slight inhibition of enzymatic activity. 
MUTAGEN   161   161        S->A: 7000-fold reduction in specific activity. 
MUTAGEN   166   166        H->G: Abolishes enzymatic activity. 
CONFLICT   29    31        AKR -> LS (in Ref. 1; CAA29574). 
TURN   6     8  3      
STRAND   11    14  4      
TURN   16    18  3      
STRAND   21    24  4      
HELIX   28    30  3      
STRAND   73    76  4      
STRAND   95    97  3      
STRAND   99   101  3      
STRAND   104   111  8      
HELIX   119   121  3      
HELIX   124   144  21      
STRAND   146   155  10      
HELIX   156   158  3      
STRAND   164   174  11      
HELIX   177   193  17      
HELIX   197   208  12      
STRAND   212   215  4      
STRAND   217   222  6      
STRAND   233   239  7      
HELIX   244   246  3      
HELIX   249   270  22      
STRAND   276   281  6      
STRAND   285   288  4      
STRAND   296   300  5      
STRAND   305   308  4      
HELIX   316   319  4      
STRAND   323   326  4      
HELIX   328   336  9      
HELIX   343   346  4      
Sequence information
Length: 348 AA [This is the length of the unprocessed precursor] Molecular weight: 39646 Da [This is the MW of the unprocessed precursor] CRC64: 3D55D2CB38D8C9A2 [This is a checksum on the sequence]
        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 

P09148 in FASTA format

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