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Glucose-1-phosphate thymidylyltransferase 1 (G1P-TT 1) (EC 2.7.7.24) (dTDP-glucose pyrophosphorylase 1) (dTDP-glucose synthase 1)

 RMLA1_ECOLI             Reviewed;         293 AA.
P37744; P78081;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
28-MAR-2018, entry version 147.
RecName: Full=Glucose-1-phosphate thymidylyltransferase 1;
Short=G1P-TT 1;
EC=2.7.7.24 {ECO:0000269|PubMed:11697907};
AltName: Full=dTDP-glucose pyrophosphorylase 1;
AltName: Full=dTDP-glucose synthase 1;
Name=rfbA; Synonyms=rmlA, rmlA1; OrderedLocusNames=b2039, JW2024;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12 / WG1;
PubMed=7517391; DOI=10.1128/jb.176.13.4144-4156.1994;
Stevenson G., Neal B., Liu D., Hobbs M., Packer N.H., Batley M.,
Redmond J.W., Lindquist L., Reeves P.R.;
"Structure of the O antigen of Escherichia coli K-12 and the sequence
of its rfb gene cluster.";
J. Bacteriol. 176:4144-4156(1994).
[2]
SEQUENCE REVISION TO 288.
Stevenson G.;
Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=9097040; DOI=10.1093/dnares/3.6.379;
Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C.,
Yamamoto Y., Horiuchi T.;
"A 460-kb DNA sequence of the Escherichia coli K-12 genome
corresponding to the 40.1-50.0 min region on the linkage map.";
DNA Res. 3:379-392(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
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 277:1453-1462(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
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).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 247-293.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=7517390; DOI=10.1128/jb.176.13.4133-4143.1994;
Yao Z., Valvano M.A.;
"Genetic analysis of the O-specific lipopolysaccharide biosynthesis
region (rfb) of Escherichia coli K-12 W3110: identification of genes
that confer group 6 specificity to Shigella flexneri serotypes Y and
4a.";
J. Bacteriol. 176:4133-4143(1994).
[7]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
PATHWAY, SUBUNIT, AND X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF
COMPLEXES WITH DTDP-G; DTMP AND G1P AND DEOXYTHYMIDINE AND G1P.
STRAIN=K12;
PubMed=11697907; DOI=10.1006/jmbi.2001.5073;
Zuccotti S., Zanardi D., Rosano C., Sturla L., Tonetti M.,
Bolognesi M.;
"Kinetic and crystallographic analyses support a sequential-ordered bi
bi catalytic mechanism for Escherichia coli glucose-1-phosphate
thymidylyltransferase.";
J. Mol. Biol. 313:831-843(2001).
-!- FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and
glucose 1-phosphate, as well as its pyrophosphorolysis.
{ECO:0000269|PubMed:11697907}.
-!- CATALYTIC ACTIVITY: dTTP + alpha-D-glucose 1-phosphate =
diphosphate + dTDP-alpha-D-glucose. {ECO:0000269|PubMed:11697907}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:11697907};
Note=Binds 1 Mg(2+) ion per subunit.
{ECO:0000269|PubMed:11697907};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=20.5 uM for dTTP {ECO:0000269|PubMed:11697907};
KM=34 uM for glucose 1-phosphate {ECO:0000269|PubMed:11697907};
KM=95 uM for dTDP-glucose {ECO:0000269|PubMed:11697907};
KM=154 uM for PPi {ECO:0000269|PubMed:11697907};
Vmax=194 umol/min/mg enzyme for the forward reaction
{ECO:0000269|PubMed:11697907};
Vmax=360 umol/min/mg enzyme for the reverse reaction
{ECO:0000269|PubMed:11697907};
pH dependence:
Optimum pH is 8.0-8.5. Active from pH 6.0 to 10.0.
{ECO:0000269|PubMed:11697907};
-!- PATHWAY: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
{ECO:0000269|PubMed:11697907}.
-!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
biosynthesis. {ECO:0000269|PubMed:11697907}.
-!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:11697907}.
-!- MISCELLANEOUS: Both catalyzed reactions, i.e. dTDP-glucose
biosynthesis and pyrophosphorolysis, follow a sequential ordered
bi-bi catalytic mechanism. {ECO:0000269|PubMed:11697907}.
-!- SIMILARITY: Belongs to the glucose-1-phosphate
thymidylyltransferase family. {ECO:0000305}.
-!- CAUTION: Most extant K-12 lines do not express O-antigen because
of mutations in dTDP-rhamnose biosynthetic genes or in the
rhamnosyltransferase gene wbbL. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U09876; AAB88400.1; -; Genomic_DNA.
EMBL; U00096; AAC75100.1; -; Genomic_DNA.
EMBL; AP009048; BAA15881.1; -; Genomic_DNA.
EMBL; U03041; AAC31629.1; -; Genomic_DNA.
PIR; F64969; F64969.
RefSeq; NP_416543.1; NC_000913.3.
RefSeq; WP_000783975.1; NZ_LN832404.1.
PDB; 1H5R; X-ray; 1.90 A; A/B/C/D=1-293.
PDB; 1H5S; X-ray; 2.30 A; A/B/C/D=1-293.
PDB; 1H5T; X-ray; 1.90 A; A/B/C/D=1-293.
PDBsum; 1H5R; -.
PDBsum; 1H5S; -.
PDBsum; 1H5T; -.
ProteinModelPortal; P37744; -.
SMR; P37744; -.
BioGrid; 4259680; 190.
IntAct; P37744; 9.
STRING; 316385.ECDH10B_2189; -.
SWISS-2DPAGE; P37744; -.
EPD; P37744; -.
PaxDb; P37744; -.
PRIDE; P37744; -.
EnsemblBacteria; AAC75100; AAC75100; b2039.
EnsemblBacteria; BAA15881; BAA15881; BAA15881.
GeneID; 945154; -.
KEGG; ecj:JW2024; -.
KEGG; eco:b2039; -.
PATRIC; fig|1411691.4.peg.212; -.
EchoBASE; EB1921; -.
EcoGene; EG11978; rfbA.
eggNOG; ENOG4108I19; Bacteria.
eggNOG; COG1209; LUCA.
HOGENOM; HOG000283473; -.
InParanoid; P37744; -.
KO; K00973; -.
OMA; GPYPMIY; -.
PhylomeDB; P37744; -.
BioCyc; EcoCyc:DTDPGLUCOSEPP-MONOMER; -.
BioCyc; MetaCyc:DTDPGLUCOSEPP-MONOMER; -.
UniPathway; UPA00124; -.
UniPathway; UPA00281; -.
EvolutionaryTrace; P37744; -.
PRO; PR:P37744; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0008879; F:glucose-1-phosphate thymidylyltransferase activity; IDA:EcoCyc.
GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
GO; GO:0046872; F:metal ion binding; IDA:EcoCyc.
GO; GO:0019305; P:dTDP-rhamnose biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; IEA:InterPro.
GO; GO:0009243; P:O antigen biosynthetic process; IEA:UniProtKB-UniPathway.
CDD; cd02538; G1P_TT_short; 1.
Gene3D; 3.90.550.10; -; 1.
InterPro; IPR005907; G1P_thy_trans_s.
InterPro; IPR005835; NTP_transferase_dom.
InterPro; IPR029044; Nucleotide-diphossugar_trans.
PANTHER; PTHR43532; PTHR43532; 1.
Pfam; PF00483; NTP_transferase; 1.
SUPFAM; SSF53448; SSF53448; 1.
TIGRFAMs; TIGR01207; rmlA; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Lipopolysaccharide biosynthesis;
Magnesium; Metal-binding; Nucleotidyltransferase; Reference proteome;
Transferase.
CHAIN 1 293 Glucose-1-phosphate thymidylyltransferase
1.
/FTId=PRO_0000207991.
METAL 111 111 Magnesium.
{ECO:0000250|UniProtKB:P61887}.
METAL 226 226 Magnesium.
{ECO:0000250|UniProtKB:P61887}.
CONFLICT 247 247 Q -> P (in Ref. 6; AAC31629).
{ECO:0000305}.
STRAND 4 9 {ECO:0000244|PDB:1H5R}.
HELIX 15 17 {ECO:0000244|PDB:1H5R}.
TURN 18 22 {ECO:0000244|PDB:1H5R}.
HELIX 26 28 {ECO:0000244|PDB:1H5R}.
STRAND 29 31 {ECO:0000244|PDB:1H5R}.
HELIX 38 46 {ECO:0000244|PDB:1H5R}.
STRAND 49 56 {ECO:0000244|PDB:1H5R}.
TURN 58 60 {ECO:0000244|PDB:1H5R}.
HELIX 61 68 {ECO:0000244|PDB:1H5R}.
HELIX 72 74 {ECO:0000244|PDB:1H5R}.
STRAND 77 82 {ECO:0000244|PDB:1H5R}.
HELIX 91 95 {ECO:0000244|PDB:1H5R}.
HELIX 97 100 {ECO:0000244|PDB:1H5R}.
STRAND 105 109 {ECO:0000244|PDB:1H5R}.
STRAND 113 115 {ECO:0000244|PDB:1H5R}.
HELIX 119 128 {ECO:0000244|PDB:1H5R}.
STRAND 131 139 {ECO:0000244|PDB:1H5R}.
HELIX 143 145 {ECO:0000244|PDB:1H5R}.
STRAND 146 151 {ECO:0000244|PDB:1H5R}.
STRAND 153 155 {ECO:0000244|PDB:1H5S}.
STRAND 157 163 {ECO:0000244|PDB:1H5R}.
STRAND 170 179 {ECO:0000244|PDB:1H5R}.
HELIX 183 189 {ECO:0000244|PDB:1H5R}.
STRAND 194 197 {ECO:0000244|PDB:1H5S}.
HELIX 200 209 {ECO:0000244|PDB:1H5R}.
STRAND 213 217 {ECO:0000244|PDB:1H5R}.
STRAND 222 225 {ECO:0000244|PDB:1H5R}.
HELIX 230 247 {ECO:0000244|PDB:1H5R}.
HELIX 254 260 {ECO:0000244|PDB:1H5R}.
HELIX 266 273 {ECO:0000244|PDB:1H5R}.
HELIX 274 276 {ECO:0000244|PDB:1H5R}.
HELIX 280 288 {ECO:0000244|PDB:1H5R}.
SEQUENCE 293 AA; 32694 MW; BA895362D1C5CA55 CRC64;
MKMRKGIILA GGSGTRLYPV TMAVSKQLLP IYDKPMIYYP LSTLMLAGIR DILIISTPQD
TPRFQQLLGD GSQWGLNLQY KVQPSPDGLA QAFIIGEEFI GGDDCALVLG DNIFYGHDLP
KLMEAAVNKE SGATVFAYHV NDPERYGVVE FDKNGTAISL EEKPLEPKSN YAVTGLYFYD
NDVVQMAKNL KPSARGELEI TDINRIYLEQ GRLSVAMMGR GYAWLDTGTH QSLIEASNFI
ATIEERQGLK VSCPEEIAFR KGFIDVEQVR KLAVPLIKNN YGQYLYKMTK DSN


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