RFBJ_SALTY
ID RFBJ_SALTY Reviewed; 299 AA.
AC P0A1P4; P0A1P5; P22716;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=CDP-abequose synthase {ECO:0000303|PubMed:2793832};
DE EC=1.1.1.341 {ECO:0000305|PubMed:2793832};
DE AltName: Full=O4 antigen;
GN Name=rfbJ; OrderedLocusNames=STM2089;
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], CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=LT2 / SL1654;
RX PubMed=2793832; DOI=10.1128/jb.171.10.5687-5693.1989;
RA Wyk P., Reeves P.R.;
RT "Identification and sequence of the gene for abequose synthase, which
RT confers antigenic specificity on group B salmonellae: homology with
RT galactose epimerase.";
RL J. Bacteriol. 171:5687-5693(1989).
RN [2]
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 [3]
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-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:0000305|PubMed:2793832};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC biosynthesis. {ECO:0000269|PubMed:2793832}.
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; X56793; CAA40123.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20993.1; -; Genomic_DNA.
DR PIR; S15307; S15307.
DR RefSeq; NP_461034.1; NC_003197.2.
DR RefSeq; WP_000143399.1; NC_003197.2.
DR AlphaFoldDB; P0A1P4; -.
DR SMR; P0A1P4; -.
DR PaxDb; P0A1P4; -.
DR EnsemblBacteria; AAL20993; AAL20993; STM2089.
DR GeneID; 1253610; -.
DR KEGG; stm:STM2089; -.
DR PATRIC; fig|99287.12.peg.2211; -.
DR HOGENOM; CLU_007383_1_7_6; -.
DR OMA; ATCYGRN; -.
DR PhylomeDB; P0A1P4; -.
DR BioCyc; MetaCyc:MON-13793; -.
DR BioCyc; SENT99287:STM2089-MON; -.
DR BRENDA; 1.1.1.341; 5542.
DR UniPathway; UPA00281; -.
DR Proteomes; UP000001014; Chromosome.
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; Reference proteome.
FT CHAIN 1..299
FT /note="CDP-abequose synthase"
FT /id="PRO_0000183259"
FT ACT_SITE 134
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 299 AA; 34106 MW; 92598AE849AF452C CRC64;
MTFLKEYVIV SGASGFIGKH LLEALKKSGI SVVAITRDVI KNNSNALANV RWCSWDNIEL
LVEELSIDSA LIGIIHLATE YGHKTSSLIN IEDANVIKPL KLLDLAIKYR ADIFLNTDSF
FAKKDFNYQH MRPYIITKRH FDEIGHYYAN MHDISFVNMR LEHVYGPGDG ENKFIPYIID
CLNKKQSCVK CTTGEQIRDF IFVDDVVNAY LTILENRKEV PSYTEYQVGT GAGVSLKDFL
VYLQNTMMPG SSSIFEFGAI EQRDNEIMFS VANNKNLKAM GWKPNFDYKK GIEELLKRL
