ID   RMLA_XANCP              Reviewed;         295 AA.
AC   P0C7J4; P55256;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   16-JUN-2009, entry version 11.
DE   RecName: Full=Glucose-1-phosphate thymidylyltransferase;
DE            EC=2.7.7.24;
DE   AltName: Full=dTDP-glucose synthase;
DE   AltName: Full=dTDP-glucose pyrophosphorylase;
GN   Name=rmlA; OrderedLocusNames=XCC0622;
OS   Xanthomonas campestris pv. campestris.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=340;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33913 / NCPPB 528 / LMG 568;
RX   MEDLINE=22022145; PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A.,
RA   Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C.,
RA   Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F.,
RA   Ciapina L.P., Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R.,
RA   El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C.,
RA   Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A.,
RA   Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F.,
RA   Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M.,
RA   Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H.,
RA   Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R.,
RA   Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F.,
RA   Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D.,
RA   Trindade dos Santos M., Truffi D., Tsai S.M., White F.F.,
RA   Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing
RT   host specificities.";
RL   Nature 417:459-463(2002).
CC   -!- FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and
CC       glucose 1-phosphate, as well as its pyrophosphorolysis (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: dTTP + alpha-D-glucose 1-phosphate =
CC       diphosphate + dTDP-glucose.
CC   -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
CC   -!- PATHWAY: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC       biosynthesis.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SIMILARITY: Belongs to the glucose-1-phosphate
CC       thymidylyltransferase family.
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DR   EMBL; AE012160; AAM39938.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_636014.1; -.
DR   HSSP; P37744; 1H5R.
DR   GeneID; 1001156; -.
DR   GenomeReviews; AE008922_GR; XCC0622.
DR   KEGG; xcc:XCC0622; -.
DR   OMA; P0C7J4; GMNIQYA.
DR   GO; GO:0008879; F:glucose-1-phosphate thymidylyltransferase a...; IEA:EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0045226; P:extracellular polysaccharide biosynthetic p...; IEA:InterPro.
DR   GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR005907; G1P_thy_trans_l.
DR   InterPro; IPR005835; NTP_transferase.
DR   Pfam; PF00483; NTP_transferase; 1.
DR   TIGRFAMs; TIGR01207; rmlA; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Lipopolysaccharide biosynthesis; Magnesium;
KW   Metal-binding; Nucleotidyltransferase; Transferase.
FT   CHAIN         1    295       Glucose-1-phosphate
FT                                thymidylyltransferase.
FT                                /FTId=PRO_0000208001.
FT   METAL       111    111       Magnesium (By similarity).
FT   METAL       226    226       Magnesium (By similarity).
SQ   SEQUENCE   295 AA;  32508 MW;  585D239B6EAF4554 CRC64;
     MTQRKGIILA GGSGTRLYPI TKGVSKQLLP VYDKPMIYYP LSVLMLAGIR DILIINTPHE
     QALFQSLLGD GAQWGVNIQY AVQPSPDGLA QAYLIGRDFV GGKPSCLVLG DNIFHGHGLT
     DTLRRADARE QGATVFGYWV NDPERYGVAE FDQHGKVIDI AEKPEKPRSN YAVTGLYFYD
     GKASDYAAAL KPSPRGELEI TDLNRCYLDA GDLHLEPLGR GYAWLDTGTH QSLHEAANFI
     ETIQMRQGLQ VCCPEEIAFG QGWIDAEQLE RLAAPLLKND YGKYLTALAK RGAVH
//