ID   RFBJ_YERPU              Reviewed;         283 AA.
AC   Q05342;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=CDP-abequose synthase;
DE            EC=1.1.1.341;
GN   Name=rfbJ; Synonyms=abe;
OS   Yersinia pseudotuberculosis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=633;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CATALYTIC ACTIVITY.
RX   PubMed=8444803; DOI=10.1128/jb.175.5.1412-1422.1993;
RA   Kessler A.C., Haase A., Reeves P.R.;
RT   "Molecular analysis of the 3,6-dideoxyhexose pathway genes of Yersinia
RT   pseudotuberculosis serogroup IIA.";
RL   J. Bacteriol. 175:1412-1422(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8541300; DOI=10.1016/0304-4165(95)00126-3;
RA   Hobbs M., Reeves P.R.;
RT   "Genetic organisation and evolution of Yersinia pseudotuberculosis 3,6-
RT   dideoxyhexose biosynthetic genes.";
RL   Biochim. Biophys. Acta 1245:273-277(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12011023; DOI=10.1128/iai.70.6.3271-3276.2002;
RA   Pacinelli E., Wang L., Reeves P.R.;
RT   "Relationship of Yersinia pseudotuberculosis O antigens IA, IIA, and IVB:
RT   the IIA gene cluster was derived from that of IVB.";
RL   Infect. Immun. 70:3271-3276(2002).
RN   [4]
RP   IDENTIFICATION, AND FUNCTION.
RX   PubMed=1724263; DOI=10.1099/00221287-137-12-2689;
RA   Kessler A.C., Brown P.K., Romana L.K., Reeves P.R.;
RT   "Molecular cloning and genetic characterization of the rfb region from
RT   Yersinia pseudotuberculosis serogroup IIA, which determines the formation
RT   of the 3,6-dideoxyhexose abequose.";
RL   J. Gen. Microbiol. 137:2689-2695(1991).
CC   -!- FUNCTION: The CDP-abequose synthase is involved in lipopolysaccharides
CC       (LPS) synthesis containing abequose which are important antigens of the
CC       cell surface responsible for the serological O specificity. Derivatives
CC       of the 3,6-dideoxyhexose group have a particular highly immunogenic
CC       character. {ECO:0000269|PubMed:1724263}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CDP-alpha-D-abequose + NADP(+) = CDP-4-dehydro-3,6-dideoxy-
CC         alpha-D-glucose + H(+) + NADPH; Xref=Rhea:RHEA:34563,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:70783, ChEBI:CHEBI:70784; EC=1.1.1.341;
CC         Evidence={ECO:0000269|PubMed:8444803};
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; AF461770; AAB49402.1; -; Genomic_DNA.
DR   PIR; F47070; F47070.
DR   RefSeq; WP_038400274.1; NZ_UHJE01000001.1.
DR   AlphaFoldDB; Q05342; -.
DR   SMR; Q05342; -.
DR   STRING; 633.DJ40_1357; -.
DR   KEGG; ag:AAB49402; -.
DR   KEGG; ypq:DJ40_1357; -.
DR   KEGG; ypr:BZ20_1044; -.
DR   PATRIC; fig|633.44.peg.1459; -.
DR   eggNOG; COG0451; Bacteria.
DR   BRENDA; 1.1.1.341; 4560.
DR   UniPathway; UPA00281; -.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009243; P:O antigen biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR001509; Epimerase_deHydtase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF01370; Epimerase; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   1: Evidence at protein level;
KW   Lipopolysaccharide biosynthesis; NADP; Oxidoreductase.
FT   CHAIN           1..283
FT                   /note="CDP-abequose synthase"
FT                   /id="PRO_0000424185"
FT   ACT_SITE        129
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         7..13
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         48..49
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         129
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         133
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   283 AA;  32018 MW;  2A8E6D4C5AB3B6E3 CRC64;
     MRIVLTGGSG YIGSSLTPVL IKKYGRVYNI GRNTISEVSI NGSKEYCEFT YESLFDSLVE
     LSPDLVINLA AGYYNDSGAP DLNVIDGNLK IPFIILEYFK SCNYGRFINI GSYWEFSCSG
     RGVKGVNPYG IIKSTVRRLL DYYSKYNVIY TNLILYGSYG DNDHRGKIVD CIIDAVNSNE
     TLKLSPGEQK LNLVYIDDII EAILYIVSSD NGQYDNETLS IYTPTEHTVK EIVCFINEIK
     DNNLSLGGGR YRNDEVMAPD YKYRNIFHAK DKLKEYITSK IKK