RMLA3_ECOLX
ID RMLA3_ECOLX Reviewed; 293 AA.
AC P55253;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Glucose-1-phosphate thymidylyltransferase {ECO:0000303|PubMed:7559340};
DE EC=2.7.7.24 {ECO:0000269|PubMed:7559340};
DE AltName: Full=dTDP-glucose pyrophosphorylase;
DE AltName: Full=dTDP-glucose synthase;
GN Name=rmlA; Synonyms=rfbA {ECO:0000303|PubMed:7559340};
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RC STRAIN=O7:K1 / VW187;
RX PubMed=7559340; DOI=10.1128/jb.177.19.5539-5546.1995;
RA Marolda C.L., Valvano M.A.;
RT "Genetic analysis of the dTDP-rhamnose biosynthesis region of the
RT Escherichia coli VW187 (O7:K1) rfb gene cluster: identification of
RT functional homologs of rfbB and rfbA in the rff cluster and correct
RT location of the rffE gene.";
RL J. Bacteriol. 177:5539-5546(1995).
CC -!- FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and
CC glucose 1-phosphate, as well as its pyrophosphorolysis.
CC {ECO:0000269|PubMed:7559340}.
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:0000269|PubMed:7559340};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P61887};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P61887};
CC -!- PATHWAY: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
CC {ECO:0000250|UniProtKB:P61887}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC biosynthesis. {ECO:0000305|PubMed:7559340}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P61887}.
CC -!- SIMILARITY: Belongs to the glucose-1-phosphate thymidylyltransferase
CC family. {ECO:0000305}.
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DR EMBL; AF125322; AAC63614.1; -; Genomic_DNA.
DR PIR; S78544; S78544.
DR AlphaFoldDB; P55253; -.
DR SMR; P55253; -.
DR STRING; 481805.EcolC_1603; -.
DR eggNOG; COG1209; Bacteria.
DR UniPathway; UPA00124; -.
DR UniPathway; UPA00281; -.
DR GO; GO:0008879; F:glucose-1-phosphate thymidylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0019305; P:dTDP-rhamnose biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009243; P:O antigen biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd02538; G1P_TT_short; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR005907; G1P_thy_trans_s.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR43532; PTHR43532; 1.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR TIGRFAMs; TIGR01207; rmlA; 1.
PE 1: Evidence at protein level;
KW Lipopolysaccharide biosynthesis; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Transferase.
FT CHAIN 1..293
FT /note="Glucose-1-phosphate thymidylyltransferase"
FT /id="PRO_0000207993"
FT BINDING 111
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P61887"
FT BINDING 227
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P61887"
SQ SEQUENCE 293 AA; 32609 MW; 63E72272C285A88C CRC64;
MKTRKGIILA GGSGTRLYPV TMAVSKQLLP IYDKPMIYYP LSTLMLAGIR DILIISTPQD
TPRFQQLLGD GSQWGLNLQY KVQPSPDGLA QAFIIGEDFI GGDDCALVLG DNIFYGHDLP
KLMEAAVNKE SGATVFAYHV NDPERYGVVE FDNNGTAISL EEKPLEPKSN YAVTGLYFYD
NDVVEMARKN LKPSARGELE ITDINRIYME QGRLSVAMMG RGYAWLDTGT HQSLIEASNF
IATIEERQGL KVSCPEEIAY RKGFIDAEQV KVLAEPLKKN AYGQYLLKMI KGY
