RFBF_SALTI
ID RFBF_SALTI Reviewed; 257 AA.
AC Q8Z5I4; Q7CAW4;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Glucose-1-phosphate cytidylyltransferase;
DE EC=2.7.7.33;
DE AltName: Full=CDP-glucose pyrophosphorylase;
GN Name=rfbF; OrderedLocusNames=STY2302, t0780;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-257 IN COMPLEX WITH SUBSTRATE,
RP AND SUBUNIT.
RC STRAIN=CT18;
RX PubMed=15292268; DOI=10.1074/jbc.m407755200;
RA Koropatkin N.M., Holden H.M.;
RT "Molecular structure of alpha-D-glucose-1-phosphate cytidylyltransferase
RT from Salmonella typhi.";
RL J. Biol. Chem. 279:44023-44029(2004).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-257 IN COMPLEX WITH MAGNESIUM
RP AND SUBSTRATE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP SPECIFICITY, REACTION MECHANISM, SUBUNIT, AND FUNCTION.
RC STRAIN=CT18;
RX PubMed=15634670; DOI=10.1074/jbc.m414111200;
RA Koropatkin N.M., Cleland W.W., Holden H.M.;
RT "Kinetic and structural analysis of alpha-D-Glucose-1-phosphate
RT cytidylyltransferase from Salmonella typhi.";
RL J. Biol. Chem. 280:10774-10780(2005).
CC -!- FUNCTION: Involved in the biosynthesis of the tyvelose, a 3,6-
CC dideoxyhexose found in the O-antigen of the surface
CC lipopolysaccharides. It catalyzes the transfer of a CMP moiety from CTP
CC to glucose 1-phosphate. This enzyme can utilize either CTP or UTP as
CC the nucleotide donor. {ECO:0000269|PubMed:15634670}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 1-phosphate + CTP + H(+) = CDP-D-glucose +
CC diphosphate; Xref=Rhea:RHEA:18213, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:58601,
CC ChEBI:CHEBI:58660; EC=2.7.7.33;
CC Evidence={ECO:0000269|PubMed:15634670};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Note=Binds 1 Mg(2+) ion per subunit.;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=11 uM for CTP-glucose (at pH 8) {ECO:0000269|PubMed:15634670};
CC KM=52 uM for glucose 1-phosphate (at pH 8)
CC {ECO:0000269|PubMed:15634670};
CC KM=67 uM for pyrophosphate (at pH 8) {ECO:0000269|PubMed:15634670};
CC KM=148 uM for CTP (at pH 8) {ECO:0000269|PubMed:15634670};
CC KM=159 uM for UTP (at pH 8) {ECO:0000269|PubMed:15634670};
CC KM=2535 uM for UTP-glucose {ECO:0000269|PubMed:15634670};
CC KM=3000 uM for dCTP (at pH 8) {ECO:0000269|PubMed:15634670};
CC KM=3600 uM for xylose 1-phosphate (at pH 8)
CC {ECO:0000269|PubMed:15634670};
CC Vmax=15.4 umol/min/mg enzyme toward UTP (at pH 8)
CC {ECO:0000269|PubMed:15634670};
CC Vmax=110.4 umol/min/mg enzyme toward CTP (at pH 8)
CC {ECO:0000269|PubMed:15634670};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; CDP-3,6-dideoxy-D-mannose
CC biosynthesis; CDP-3,6-dideoxy-D-mannose from CTP and alpha-D-glucose 1-
CC phosphate: step 1/5.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC biosynthesis.
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:15292268,
CC ECO:0000269|PubMed:15634670}.
CC -!- MISCELLANEOUS: Catalysis proceeds via a sequential rather than a ping-
CC pong bi-bi reaction mechanism.
CC -!- SIMILARITY: Belongs to the glucose-1-phosphate cytidylyltransferase
CC family. {ECO:0000305}.
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DR EMBL; AE014613; AAO68471.1; -; Genomic_DNA.
DR EMBL; AL513382; CAD02455.1; -; Genomic_DNA.
DR RefSeq; NP_456641.1; NC_003198.1.
DR RefSeq; WP_000648783.1; NZ_WSUR01000002.1.
DR PDB; 1TZF; X-ray; 2.10 A; A=2-257.
DR PDB; 1WVC; X-ray; 2.50 A; A=2-257.
DR PDBsum; 1TZF; -.
DR PDBsum; 1WVC; -.
DR AlphaFoldDB; Q8Z5I4; -.
DR SMR; Q8Z5I4; -.
DR STRING; 220341.16503322; -.
DR BindingDB; Q8Z5I4; -.
DR ChEMBL; CHEMBL3745591; -.
DR EnsemblBacteria; AAO68471; AAO68471; t0780.
DR KEGG; stt:t0780; -.
DR KEGG; sty:STY2302; -.
DR PATRIC; fig|220341.7.peg.2322; -.
DR eggNOG; COG1208; Bacteria.
DR HOGENOM; CLU_029499_10_0_6; -.
DR OMA; YWRAIDT; -.
DR SABIO-RK; Q8Z5I4; -.
DR UniPathway; UPA00055; UER00511.
DR UniPathway; UPA00281; -.
DR EvolutionaryTrace; Q8Z5I4; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; Chromosome.
DR GO; GO:0047343; F:glucose-1-phosphate cytidylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0009243; P:O antigen biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd02524; G1P_cytidylyltransferase; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR013446; G1P_cyt_trans.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR47183:SF1; PTHR47183:SF1; 1.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR TIGRFAMs; TIGR02623; G1P_cyt_trans; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lipopolysaccharide biosynthesis; Magnesium; Metal-binding;
KW Nucleotide-binding; Nucleotidyltransferase; Transferase.
FT CHAIN 1..257
FT /note="Glucose-1-phosphate cytidylyltransferase"
FT /id="PRO_0000389446"
FT BINDING 6..10
FT /ligand="substrate"
FT BINDING 11..13
FT /ligand="substrate"
FT BINDING 23
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15292268,
FT ECO:0000269|PubMed:15634670"
FT BINDING 104
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15292268,
FT ECO:0000269|PubMed:15634670"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15292268,
FT ECO:0000269|PubMed:15634670"
FT BINDING 128
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15292268,
FT ECO:0000269|PubMed:15634670"
FT BINDING 129
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:15634670"
FT BINDING 234
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:15634670"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:1TZF"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:1WVC"
FT HELIX 15..18
FT /evidence="ECO:0007829|PDB:1WVC"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:1TZF"
FT HELIX 33..43
FT /evidence="ECO:0007829|PDB:1TZF"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:1TZF"
FT HELIX 57..65
FT /evidence="ECO:0007829|PDB:1TZF"
FT HELIX 67..71
FT /evidence="ECO:0007829|PDB:1TZF"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:1TZF"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:1TZF"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:1TZF"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:1TZF"
FT HELIX 106..112
FT /evidence="ECO:0007829|PDB:1TZF"
FT HELIX 113..116
FT /evidence="ECO:0007829|PDB:1TZF"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:1TZF"
FT STRAND 123..127
FT /evidence="ECO:0007829|PDB:1TZF"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:1TZF"
FT HELIX 136..146
FT /evidence="ECO:0007829|PDB:1TZF"
FT STRAND 149..155
FT /evidence="ECO:0007829|PDB:1TZF"
FT STRAND 161..167
FT /evidence="ECO:0007829|PDB:1TZF"
FT STRAND 170..177
FT /evidence="ECO:0007829|PDB:1TZF"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:1TZF"
FT HELIX 194..199
FT /evidence="ECO:0007829|PDB:1TZF"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:1TZF"
FT HELIX 210..217
FT /evidence="ECO:0007829|PDB:1TZF"
FT STRAND 221..226
FT /evidence="ECO:0007829|PDB:1TZF"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:1TZF"
FT HELIX 236..247
FT /evidence="ECO:0007829|PDB:1TZF"
SQ SEQUENCE 257 AA; 29007 MW; 2B0B30E61067E40D CRC64;
MKAVILAGGL GTRLSEETIV KPKPMVEIGG KPILWHIMKM YSVHGIKDFI ICCGYKGYVI
KEYFANYFLH MSDVTFHMAE NRMEVHHKRV EPWNVTLVDT GDSSMTGGRL KRVAEYVKDD
EAFLFTYGDG VADLDIKATI DFHKAHGKKA TLTATFPPGR FGALDIQAGQ VRSFQEKPKG
DGAMINGGFF VLNPSVIDLI DNDATTWEQE PLMTLAQQGE LMAFEHPGFW QPMDTLRDKV
YLEGLWEKGK APWKTWE
