RFBE_SALTI
ID RFBE_SALTI Reviewed; 338 AA.
AC P14169;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=CDP-paratose 2-epimerase;
DE EC=5.1.3.10;
DE AltName: Full=CDP-tyvelose 2-epimerase;
GN Name=rfbE; OrderedLocusNames=STY2298, t0784;
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 SEQUENCE REVISION.
RA Reeves P.R.;
RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 2-338 IN COMPLEX WITH NAD AND
RP SUBSTRATE, AND SUBUNIT.
RX PubMed=12642575; DOI=10.1074/jbc.m301948200;
RA Koropatkin N.M., Liu H.-W., Holden H.M.;
RT "High resolution X-ray structure of tyvelose epimerase from Salmonella
RT typhi.";
RL J. Biol. Chem. 278:20874-20881(2003).
CC -!- FUNCTION: Catalyzes the isomeration of CDP-paratose to CDP-tyvelose.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CDP-alpha-D-paratose = CDP-3,6-dideoxy-alpha-D-mannose;
CC Xref=Rhea:RHEA:21656, ChEBI:CHEBI:70785, ChEBI:CHEBI:88041;
CC EC=5.1.3.10;
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Note=Binds 1 NAD(+) per subunit.;
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 5/5.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:12642575}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. {ECO:0000305}.
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DR EMBL; M29682; AAB49384.1; -; Genomic_DNA.
DR EMBL; AL513382; CAD02451.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO68475.1; -; Genomic_DNA.
DR PIR; B33604; B33604.
DR RefSeq; NP_456637.1; NC_003198.1.
DR RefSeq; WP_000770936.1; NZ_WSUR01000002.1.
DR PDB; 1ORR; X-ray; 1.50 A; A/B/C/D=2-338.
DR PDBsum; 1ORR; -.
DR AlphaFoldDB; P14169; -.
DR SMR; P14169; -.
DR STRING; 220341.16503318; -.
DR DrugBank; DB04555; Cytidine-5'-Diphosphate.
DR EnsemblBacteria; AAO68475; AAO68475; t0784.
DR KEGG; stt:t0784; -.
DR KEGG; sty:STY2298; -.
DR PATRIC; fig|220341.7.peg.2318; -.
DR eggNOG; COG0451; Bacteria.
DR HOGENOM; CLU_007383_1_7_6; -.
DR OMA; MGTEDQG; -.
DR BioCyc; MetaCyc:MON-13795; -.
DR UniPathway; UPA00055; UER00515.
DR EvolutionaryTrace; P14169; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; Chromosome.
DR GO; GO:0047732; F:CDP-abequose epimerase activity; IEA:UniProtKB-EC.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF16363; GDP_Man_Dehyd; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Isomerase; Lipopolysaccharide biosynthesis.
FT CHAIN 1..338
FT /note="CDP-paratose 2-epimerase"
FT /id="PRO_0000183260"
FT ACT_SITE 164
FT /note="Proton acceptor"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12642575"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:1ORR"
FT TURN 7..9
FT /evidence="ECO:0007829|PDB:1ORR"
FT HELIX 11..22
FT /evidence="ECO:0007829|PDB:1ORR"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:1ORR"
FT HELIX 38..46
FT /evidence="ECO:0007829|PDB:1ORR"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:1ORR"
FT HELIX 61..71
FT /evidence="ECO:0007829|PDB:1ORR"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:1ORR"
FT HELIX 85..90
FT /evidence="ECO:0007829|PDB:1ORR"
FT HELIX 92..113
FT /evidence="ECO:0007829|PDB:1ORR"
FT STRAND 118..124
FT /evidence="ECO:0007829|PDB:1ORR"
FT HELIX 125..128
FT /evidence="ECO:0007829|PDB:1ORR"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:1ORR"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:1ORR"
FT HELIX 162..182
FT /evidence="ECO:0007829|PDB:1ORR"
FT STRAND 185..191
FT /evidence="ECO:0007829|PDB:1ORR"
FT HELIX 207..219
FT /evidence="ECO:0007829|PDB:1ORR"
FT STRAND 226..232
FT /evidence="ECO:0007829|PDB:1ORR"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:1ORR"
FT HELIX 241..253
FT /evidence="ECO:0007829|PDB:1ORR"
FT HELIX 255..258
FT /evidence="ECO:0007829|PDB:1ORR"
FT STRAND 262..267
FT /evidence="ECO:0007829|PDB:1ORR"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:1ORR"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:1ORR"
FT HELIX 275..286
FT /evidence="ECO:0007829|PDB:1ORR"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:1ORR"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:1ORR"
FT HELIX 310..316
FT /evidence="ECO:0007829|PDB:1ORR"
FT HELIX 324..337
FT /evidence="ECO:0007829|PDB:1ORR"
SQ SEQUENCE 338 AA; 37958 MW; 031175EDCF533888 CRC64;
MKLLITGGCG FLGSNLASFA LSQGIDLIVF DNLSRKGATD NLHWLSSLGN FEFVHGDIRN
KNDVTRLITK YMPDSCFHLA GQVAMTTSID NPCMDFEINV GGTLNLLEAV RQYNSNCNII
YSSTNKVYGD LEQYKYNETE TRYTCVDKPN GYDESTQLDF HSPYGCSKGA ADQYMLDYAR
IFGLNTVVFR HSSMYGGRQF ATYDQGWVGW FCQKAVEIKN GINKPFTISG NGKQVRDVLH
AEDMISLYFT ALANVSKIRG NAFNIGGTIV NSLSLLELFK LLEDYCNIDM RFTNLPVRES
DQRVFVADIK KITNAIDWSP KVSAKDGVQK MYDWTSSI
