RMLA2_ECOLI
ID RMLA2_ECOLI Reviewed; 293 AA.
AC P61887; P27831; P76755; Q2M897;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Glucose-1-phosphate thymidylyltransferase 2;
DE Short=G1P-TT 2;
DE EC=2.7.7.24 {ECO:0000269|PubMed:7559340};
DE AltName: Full=dTDP-glucose pyrophosphorylase 2;
DE AltName: Full=dTDP-glucose synthase 2;
GN Name=rffH; Synonyms=rmlA2, yifG; OrderedLocusNames=b3789, JW3763;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=1379743; DOI=10.1126/science.1379743;
RA Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.;
RT "Analysis of the Escherichia coli genome: DNA sequence of the region from
RT 84.5 to 86.5 minutes.";
RL Science 257:771-778(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=K12;
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).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF COMPLEX WITH DTTP, COFACTOR, AND
RP SUBUNIT.
RX PubMed=12171937; DOI=10.1074/jbc.m206932200;
RA Sivaraman J., Sauve V., Matte A., Cygler M.;
RT "Crystal structure of Escherichia coli glucose-1-phosphate
RT thymidylyltransferase (RffH) complexed with dTTP and Mg2+.";
RL J. Biol. Chem. 277:44214-44219(2002).
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:0000269|PubMed:12171937};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:12171937};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; dTDP-4-acetamido-4,6-
CC dideoxygalactose biosynthesis. {ECO:0000269|PubMed:7559340}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; enterobacterial common
CC antigen biosynthesis. {ECO:0000269|PubMed:7559340}.
CC -!- SUBUNIT: Homotetramer; arranged as a dimer of dimers.
CC {ECO:0000269|PubMed:12171937}.
CC -!- SIMILARITY: Belongs to the glucose-1-phosphate thymidylyltransferase
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M87049; AAA67589.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76794.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77509.1; -; Genomic_DNA.
DR PIR; H65182; H65182.
DR RefSeq; NP_418236.1; NC_000913.3.
DR RefSeq; WP_000676056.1; NZ_STEB01000021.1.
DR PDB; 1MC3; X-ray; 2.60 A; A/B=1-293.
DR PDBsum; 1MC3; -.
DR AlphaFoldDB; P61887; -.
DR SMR; P61887; -.
DR BioGRID; 4261364; 234.
DR DIP; DIP-10689N; -.
DR IntAct; P61887; 5.
DR STRING; 511145.b3789; -.
DR jPOST; P61887; -.
DR PaxDb; P61887; -.
DR PRIDE; P61887; -.
DR EnsemblBacteria; AAC76794; AAC76794; b3789.
DR EnsemblBacteria; BAE77509; BAE77509; BAE77509.
DR GeneID; 66672308; -.
DR GeneID; 948299; -.
DR KEGG; ecj:JW3763; -.
DR KEGG; eco:b3789; -.
DR PATRIC; fig|1411691.4.peg.2917; -.
DR EchoBASE; EB1423; -.
DR eggNOG; COG1209; Bacteria.
DR HOGENOM; CLU_029499_9_0_6; -.
DR InParanoid; P61887; -.
DR OMA; ITHAIQW; -.
DR PhylomeDB; P61887; -.
DR BioCyc; EcoCyc:DTDPGLUCOSEPP2-MON; -.
DR BioCyc; MetaCyc:DTDPGLUCOSEPP2-MON; -.
DR UniPathway; UPA00566; -.
DR UniPathway; UPA00817; -.
DR EvolutionaryTrace; P61887; -.
DR PRO; PR:P61887; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0008879; F:glucose-1-phosphate thymidylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0009246; P:enterobacterial common antigen biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; IDA:UniProtKB.
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 3D-structure; Exopolysaccharide synthesis; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Reference proteome; Transferase.
FT CHAIN 1..293
FT /note="Glucose-1-phosphate thymidylyltransferase 2"
FT /id="PRO_0000207992"
FT BINDING 108
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:12171937"
FT BINDING 223
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:12171937"
FT CONFLICT 5
FT /note="I -> M (in Ref. 1; AAA67589)"
FT /evidence="ECO:0000305"
FT CONFLICT 68..69
FT /note="GS -> VG (in Ref. 1; AAA67589)"
FT /evidence="ECO:0000305"
FT CONFLICT 130..131
FT /note="AT -> P (in Ref. 1; AAA67589)"
FT /evidence="ECO:0000305"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:1MC3"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:1MC3"
FT HELIX 15..18
FT /evidence="ECO:0007829|PDB:1MC3"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:1MC3"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:1MC3"
FT HELIX 35..43
FT /evidence="ECO:0007829|PDB:1MC3"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:1MC3"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:1MC3"
FT HELIX 58..65
FT /evidence="ECO:0007829|PDB:1MC3"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:1MC3"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:1MC3"
FT HELIX 88..92
FT /evidence="ECO:0007829|PDB:1MC3"
FT HELIX 94..97
FT /evidence="ECO:0007829|PDB:1MC3"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:1MC3"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:1MC3"
FT HELIX 117..123
FT /evidence="ECO:0007829|PDB:1MC3"
FT STRAND 128..136
FT /evidence="ECO:0007829|PDB:1MC3"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:1MC3"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:1MC3"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:1MC3"
FT STRAND 167..175
FT /evidence="ECO:0007829|PDB:1MC3"
FT HELIX 179..185
FT /evidence="ECO:0007829|PDB:1MC3"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:1MC3"
FT HELIX 197..206
FT /evidence="ECO:0007829|PDB:1MC3"
FT STRAND 210..214
FT /evidence="ECO:0007829|PDB:1MC3"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:1MC3"
FT HELIX 227..244
FT /evidence="ECO:0007829|PDB:1MC3"
FT HELIX 251..257
FT /evidence="ECO:0007829|PDB:1MC3"
FT HELIX 263..272
FT /evidence="ECO:0007829|PDB:1MC3"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:1MC3"
FT HELIX 277..284
FT /evidence="ECO:0007829|PDB:1MC3"
SQ SEQUENCE 293 AA; 32734 MW; 5DA66676CD8F9139 CRC64;
MKGIILAGGS GTRLHPITRG VSKQLLPIYD KPMIYYPLSV LMLAGIREIL IITTPEDKGY
FQRLLGDGSE FGIQLEYAEQ PSPDGLAQAF IIGETFLNGE PSCLVLGDNI FFGQGFSPKL
RHVAARTEGA TVFGYQVMDP ERFGVVEFDD NFRAISLEEK PKQPKSNWAV TGLYFYDSKV
VEYAKQVKPS ERGELEITSI NQMYLEAGNL TVELLGRGFA WLDTGTHDSL IEASTFVQTV
EKRQGFKIAC LEEIAWRNGW LDDEGVKRAA SSLAKTGYGQ YLLELLRARP RQY
