ID D7PDW1_ECOLX Unreviewed; 291 AA.
AC D7PDW1;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE RecName: Full=Glucose-1-phosphate thymidylyltransferase {ECO:0000256|ARBA:ARBA00012461, ECO:0000256|RuleBase:RU003706};
DE EC=2.7.7.24 {ECO:0000256|ARBA:ARBA00012461, ECO:0000256|RuleBase:RU003706};
GN Name=rmlA {ECO:0000313|EMBL:ADC54947.1};
OS Escherichia coli.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562 {ECO:0000313|EMBL:ADC54947.1};
RN [1] {ECO:0000313|EMBL:ADC54947.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=G1630 {ECO:0000313|EMBL:ADC54947.1};
RX PubMed=20434495; DOI=10.1016/j.mimet.2010.04.008;
RA Li D., Liu B., Chen M., Guo D., Guo X., Liu F., Feng L., Wang L.;
RT "A multiplex PCR method to detect 14 Escherichia coli serogroups associated
RT with urinary tract infections.";
RL J. Microbiol. Methods 82:71-77(2010).
RN [2] {ECO:0000313|EMBL:BAQ00684.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=D-M3219-54 {ECO:0000313|EMBL:BAQ00684.1};
RA Iguchi A., Iyoda S., Kikuchi T., Ogura Y., Katsura K., Ohnishi M.,
RA Hayashi T., Thomson N.R.;
RT "A complete view of the genetic diversity of the Escherichia coli O-antigen
RT biosynthesis gene cluster.";
RL DNA Res. 0:0-0(2014).
CC -!- FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and
CC glucose 1-phosphate, as well as its pyrophosphorolysis.
CC {ECO:0000256|RuleBase:RU003706}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 1-phosphate + dTTP + H(+) = diphosphate +
CC dTDP-alpha-D-glucose; Xref=Rhea:RHEA:15225, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37568, ChEBI:CHEBI:57477,
CC ChEBI:CHEBI:58601; EC=2.7.7.24;
CC Evidence={ECO:0000256|ARBA:ARBA00001095,
CC ECO:0000256|RuleBase:RU003706};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC biosynthesis. {ECO:0000256|ARBA:ARBA00005125}.
CC -!- PATHWAY: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004781}.
CC -!- SIMILARITY: Belongs to the glucose-1-phosphate thymidylyltransferase
CC family. {ECO:0000256|ARBA:ARBA00010480, ECO:0000256|RuleBase:RU003706}.
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DR EMBL; GU299793; ADC54947.1; -; Genomic_DNA.
DR EMBL; AB811603; BAQ00684.1; -; Genomic_DNA.
DR RefSeq; WP_000857501.1; NZ_WJQX01000001.1.
DR AlphaFoldDB; D7PDW1; -.
DR PATRIC; fig|562.7268.peg.3500; -.
DR OMA; PFIMYLG; -.
DR GO; GO:0008879; F:glucose-1-phosphate thymidylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; IEA:InterPro.
DR CDD; cd02538; G1P_TT_short; 1.
DR InterPro; IPR005907; G1P_thy_trans_s.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR NCBIfam; TIGR01207; rmlA; 1.
DR PANTHER; PTHR43532; GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE; 1.
DR PANTHER; PTHR43532:SF1; GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE 1; 1.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|RuleBase:RU003706};
KW Metal-binding {ECO:0000256|RuleBase:RU003706};
KW Nucleotidyltransferase {ECO:0000256|RuleBase:RU003706};
KW Transferase {ECO:0000256|RuleBase:RU003706, ECO:0000313|EMBL:BAQ00684.1}.
FT DOMAIN 5..241
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 291 AA; 32341 MW; 3D6A2B07A708D95D CRC64;
MKTRKGIILA GGSGTRLYPV TMAVSKQLLP IYDKPMIYYP LSTLMLAGIR DILIISTPQD
TPRFQQLLGD GSQWGLNLHY KVQPSPDGLA QAFIIGEEFI GGDDCALVLG DNIFYGHDLP
KLMDAAVNKE SGATVFAYHV NDPERYGVVE FDKNGTAISL EEKPLQPKSN YAVTGLYFYD
NYVVEMAKNL KPSARGELEI TDINRIYMEQ GHLSVAMMGR GYAWLDTGTH QSLIEASNFI
ATIEERQGLK VSCPEEIAYR KGFIDAEQVK VLAEPLKKNA YGQYLLKMIK G
//