ID   RFBS_SALTI              Reviewed;         279 AA.
AC   P14168;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   05-DEC-2001, sequence version 2.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=CDP-paratose synthase;
DE            EC=1.1.1.342;
GN   Name=rfbS; OrderedLocusNames=STY2299, t0783;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=2793833; DOI=10.1128/jb.171.10.5694-5701.1989;
RA   Verma N., Reeves P.R.;
RT   "Identification and sequence of rfbS and rfbE, which determine antigenic
RT   specificity of group A and group D salmonellae.";
RL   J. Bacteriol. 171:5694-5701(1989).
RN   [2]
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   [3]
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).
CC   -!- FUNCTION: Catalyzes synthesis of paratose and tyvelose, unusual 3,6-
CC       dideoxyhexose sugars that form part of the O-antigen in the
CC       lipopolysaccharides of several enteric bacteria.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CDP-alpha-D-paratose + NADP(+) = CDP-4-dehydro-3,6-dideoxy-
CC         alpha-D-glucose + H(+) + NADPH; Xref=Rhea:RHEA:34567,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:70783, ChEBI:CHEBI:70785; EC=1.1.1.342;
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 4/5.
CC   -!- MISCELLANEOUS: The functional difference between abequose synthase and
CC       paratose synthase lies in the side of the pyranose ring from which the
CC       keto group on carbon 4 is attacked in the reduction of CDP-4-keto-3,6-
CC       dideoxy-D-glucose.
CC   -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC       family. {ECO:0000305}.
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DR   EMBL; M29682; AAB49383.1; -; Genomic_DNA.
DR   EMBL; AL513382; CAD02452.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO68474.1; -; Genomic_DNA.
DR   RefSeq; NP_456638.1; NC_003198.1.
DR   RefSeq; WP_000697757.1; NZ_WSUR01000002.1.
DR   AlphaFoldDB; P14168; -.
DR   SMR; P14168; -.
DR   STRING; 220341.16503319; -.
DR   EnsemblBacteria; AAO68474; AAO68474; t0783.
DR   KEGG; stt:t0783; -.
DR   KEGG; sty:STY2299; -.
DR   PATRIC; fig|220341.7.peg.2319; -.
DR   eggNOG; COG0451; Bacteria.
DR   HOGENOM; CLU_007383_1_7_6; -.
DR   OMA; ATCYGRN; -.
DR   BioCyc; MetaCyc:MON-13794; -.
DR   BRENDA; 1.1.1.342; 5557.
DR   UniPathway; UPA00055; UER00514.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR001509; Epimerase_deHydtase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF01370; Epimerase; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   3: Inferred from homology;
KW   Lipopolysaccharide biosynthesis; NADP; Oxidoreductase.
FT   CHAIN           1..279
FT                   /note="CDP-paratose synthase"
FT                   /id="PRO_0000183265"
FT   ACT_SITE        115
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        120
FT                   /note="Q -> T (in Ref. 1; AAB49383)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   279 AA;  31501 MW;  6C2E83487FF444EB CRC64;
     MKILIMGAFG FLGSRLTSYF ESRHTVIGLA RKRNNEATIN NIIYTTENNW IEKILEFEPN
     IIINTIACYG RHNEPATALI ESNILMPIRV LESISSLDAV FINCGTSLPP NTSLYAYTKQ
     KANELAAAII DKVCGKYIEL KLEHFYGAFD GDDKFTSMVI RRCLSNQPVK LTSGLQQRDF
     LYIKDLLTAF DCIISNVNNF PKFHSIEVGS GEAISIREYV DTVKNITKSN SIIEFGVVKE
     RVNELMYSCA DIAELEKIGW KREFSLVDAL TEIIEEEGK