RFBF_SALTY
ID RFBF_SALTY Reviewed; 257 AA.
AC P26396;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Glucose-1-phosphate cytidylyltransferase;
DE EC=2.7.7.33;
DE AltName: Full=CDP-glucose pyrophosphorylase;
GN Name=rfbF; OrderedLocusNames=STM2092;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=1710759; DOI=10.1111/j.1365-2958.1991.tb00741.x;
RA Jiang X.-M., Neal B., Santiago F., Lee S.J., Romana L.K., Reeves P.R.;
RT "Structure and sequence of the rfb (O antigen) gene cluster of Salmonella
RT serovar typhimurium (strain LT2).";
RL Mol. Microbiol. 5:695-713(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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 (By similarity). {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
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:0000250}.
CC -!- MISCELLANEOUS: Catalysis proceeds via a sequential rather than a ping-
CC pong bi-bi reaction mechanism. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glucose-1-phosphate cytidylyltransferase
CC family. {ECO:0000305}.
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DR EMBL; X56793; CAA40120.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20996.1; -; Genomic_DNA.
DR PIR; S15304; S15304.
DR RefSeq; NP_461037.1; NC_003197.2.
DR RefSeq; WP_000648784.1; NC_003197.2.
DR AlphaFoldDB; P26396; -.
DR SMR; P26396; -.
DR STRING; 99287.STM2092; -.
DR DrugBank; DB02431; Cytidine-5'-Triphosphate.
DR PaxDb; P26396; -.
DR EnsemblBacteria; AAL20996; AAL20996; STM2092.
DR GeneID; 1253613; -.
DR KEGG; stm:STM2092; -.
DR PATRIC; fig|99287.12.peg.2214; -.
DR HOGENOM; CLU_029499_10_0_6; -.
DR OMA; YWRAIDT; -.
DR PhylomeDB; P26396; -.
DR BioCyc; SENT99287:STM2092-MON; -.
DR UniPathway; UPA00055; UER00511.
DR UniPathway; UPA00281; -.
DR Proteomes; UP000001014; 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 3: Inferred from homology;
KW Lipopolysaccharide biosynthesis; Magnesium; Metal-binding;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..257
FT /note="Glucose-1-phosphate cytidylyltransferase"
FT /id="PRO_0000097293"
FT BINDING 6..10
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 11..13
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 23
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 234
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 257 AA; 29035 MW; 04DB33D51357D70E CRC64;
MKAVILAGGL GTRLSEETIV KPKPMVEIGG KPILWHIMKM YSVHGIKDFI ICCGYKGYVI
KEYFANYFLH MSDVTFHMAE NRMEVHHKRV EPWNVTLVDT GDSSMTGGRL KRVAEYVKDD
EAFLFTYGDG VADLDIKATI DFHKAHGKKA TLTATFPPGR FGALDIRAGQ VRSFQEKPKG
DGAMINGGFF VLNPSVIDLI DNDATTWEQE PLMTLAQQGE LMAFEHPGFW QPMDTLRDKV
YLEGLWEKGK APWKTWE
