ID RFBG_SALTY Reviewed; 359 AA.
AC P26397;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 27-MAR-2024, entry version 138.
DE RecName: Full=CDP-glucose 4,6-dehydratase;
DE EC=4.2.1.45;
GN Name=rfbG; OrderedLocusNames=STM2091;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Pseudomonadota; 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 -!- CATALYTIC ACTIVITY:
CC Reaction=CDP-D-glucose = CDP-4-dehydro-6-deoxy-D-glucose + H2O;
CC Xref=Rhea:RHEA:17153, ChEBI:CHEBI:15377, ChEBI:CHEBI:58166,
CC ChEBI:CHEBI:58660; EC=4.2.1.45;
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
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 2/5.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC biosynthesis.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. {ECO:0000305}.
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DR EMBL; X56793; CAA40121.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20995.1; -; Genomic_DNA.
DR PIR; S15305; S15305.
DR RefSeq; NP_461036.1; NC_003197.2.
DR RefSeq; WP_000565905.1; NC_003197.2.
DR PDB; 1WVG; X-ray; 1.80 A; A/B=2-359.
DR PDBsum; 1WVG; -.
DR AlphaFoldDB; P26397; -.
DR SMR; P26397; -.
DR STRING; 99287.STM2091; -.
DR DrugBank; DB02059; Adenosine-5-Diphosphoribose.
DR DrugBank; DB03069; Cytidine-5'-diphospho-beta-D-xylose.
DR PaxDb; 99287-STM2091; -.
DR GeneID; 1253612; -.
DR KEGG; stm:STM2091; -.
DR PATRIC; fig|99287.12.peg.2213; -.
DR HOGENOM; CLU_007383_1_7_6; -.
DR OMA; CYENREW; -.
DR PhylomeDB; P26397; -.
DR BioCyc; SENT99287:STM2091-MONOMER; -.
DR UniPathway; UPA00055; UER00512.
DR UniPathway; UPA00281; -.
DR EvolutionaryTrace; P26397; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0047733; F:CDP-glucose 4,6-dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0009243; P:O antigen biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd05252; CDP_GD_SDR_e; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.90.25.10; UDP-galactose 4-epimerase, domain 1; 1.
DR InterPro; IPR013445; CDP_4_6_deHydtase.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR02622; CDP_4_6_dhtase; 1.
DR PANTHER; PTHR43000:SF7; DTDP-D-GLUCOSE 4,6-DEHYDRATASE; 1.
DR PANTHER; PTHR43000; DTDP-D-GLUCOSE 4,6-DEHYDRATASE-RELATED; 1.
DR Pfam; PF16363; GDP_Man_Dehyd; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lipopolysaccharide biosynthesis; Lyase; NAD;
KW Reference proteome.
FT CHAIN 1..359
FT /note="CDP-glucose 4,6-dehydratase"
FT /id="PRO_0000097294"
FT HELIX 4..7
FT /evidence="ECO:0007829|PDB:1WVG"
FT STRAND 11..15
FT /evidence="ECO:0007829|PDB:1WVG"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:1WVG"
FT HELIX 20..31
FT /evidence="ECO:0007829|PDB:1WVG"
FT STRAND 35..42
FT /evidence="ECO:0007829|PDB:1WVG"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:1WVG"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:1WVG"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:1WVG"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:1WVG"
FT HELIX 69..79
FT /evidence="ECO:0007829|PDB:1WVG"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:1WVG"
FT HELIX 93..98
FT /evidence="ECO:0007829|PDB:1WVG"
FT HELIX 100..121
FT /evidence="ECO:0007829|PDB:1WVG"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:1WVG"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:1WVG"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:1WVG"
FT HELIX 156..175
FT /evidence="ECO:0007829|PDB:1WVG"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:1WVG"
FT HELIX 181..184
FT /evidence="ECO:0007829|PDB:1WVG"
FT STRAND 187..193
FT /evidence="ECO:0007829|PDB:1WVG"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:1WVG"
FT HELIX 207..216
FT /evidence="ECO:0007829|PDB:1WVG"
FT STRAND 221..224
FT /evidence="ECO:0007829|PDB:1WVG"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:1WVG"
FT HELIX 236..251
FT /evidence="ECO:0007829|PDB:1WVG"
FT HELIX 253..256
FT /evidence="ECO:0007829|PDB:1WVG"
FT STRAND 258..262
FT /evidence="ECO:0007829|PDB:1WVG"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:1WVG"
FT HELIX 272..283
FT /evidence="ECO:0007829|PDB:1WVG"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:1WVG"
FT HELIX 308..313
FT /evidence="ECO:0007829|PDB:1WVG"
FT HELIX 322..337
FT /evidence="ECO:0007829|PDB:1WVG"
FT HELIX 342..355
FT /evidence="ECO:0007829|PDB:1WVG"
SQ SEQUENCE 359 AA; 41022 MW; D6EB7B3D36B2F9FB CRC64;
MIDKNFWQGK RVFVTGHTGF KGSWLSLWLT EMGAIVKGYA LDAPTVPSLF EIVRLNDLME
SHIGDIRDFE KLRNSIAEFK PEIVFHMAAQ PLVRLSYEQP IETYSTNVMG TVHLLETVKQ
VGNIKAVVNI TSDKCYDNRE WVWGYRENEP MGGYDPYSNS KGCAELVASA FRNSFFNPAN
YEQHGVGLAS VRAGNVIGGG DWAKDRLIPD ILRSFENNQQ VIIRNPYSIR PWQHVLEPLS
GYIVVAQRLY TEGAKFSEGW NFGPRDEDAK TVEFIVDKMV TLWGDDASWL LDGENHPHEA
HYLKLDCSKA NMQLGWHPRW GLTETLGRIV KWHKAWIRGE DMLICSKREI SDYMSATTR
//
