RMLB_SHIFL
ID RMLB_SHIFL Reviewed; 361 AA.
AC P37777; Q54162;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=dTDP-glucose 4,6-dehydratase {ECO:0000250|UniProtKB:P27830};
DE EC=4.2.1.46 {ECO:0000250|UniProtKB:P27830};
GN Name=rfbB; OrderedLocusNames=SF2104, S2227;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PE577 / Serotype 2a;
RX PubMed=8170390; DOI=10.1111/j.1365-2958.1994.tb00308.x;
RA Macpherson D.F., Manning P.A., Morona R.;
RT "Characterization of the dTDP-rhamnose biosynthetic genes encoded in the
RT rfb locus of Shigella flexneri.";
RL Mol. Microbiol. 11:281-292(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=YSH6200 / Serotype 2a;
RX PubMed=8157605; DOI=10.1128/jb.176.8.2362-2373.1994;
RA Rajakumar K., Jost B.H., Sasakawa C., Okada N., Yoshikawa M., Adler B.;
RT "Nucleotide sequence of the rhamnose biosynthetic operon of Shigella
RT flexneri 2a and role of lipopolysaccharide in virulence.";
RL J. Bacteriol. 176:2362-2373(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
CC -!- FUNCTION: Catalyzes the dehydration of dTDP-D-glucose to form dTDP-6-
CC deoxy-D-xylo-4-hexulose via a three-step process involving oxidation,
CC dehydration and reduction. {ECO:0000250|UniProtKB:P27830}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dTDP-alpha-D-glucose = dTDP-4-dehydro-6-deoxy-alpha-D-glucose
CC + H2O; Xref=Rhea:RHEA:17221, ChEBI:CHEBI:15377, ChEBI:CHEBI:57477,
CC ChEBI:CHEBI:57649; EC=4.2.1.46;
CC Evidence={ECO:0000250|UniProtKB:P27830};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000250|UniProtKB:P27830};
CC Note=Binds 1 NAD(+) per subunit. {ECO:0000250|UniProtKB:P27830};
CC -!- PATHWAY: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
CC {ECO:0000250|UniProtKB:P37759}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC biosynthesis. {ECO:0000250|UniProtKB:P37759}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P27830}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. dTDP-glucose dehydratase subfamily.
CC {ECO:0000250|UniProtKB:P27830}.
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DR EMBL; X71970; CAA50767.1; -; Genomic_DNA.
DR EMBL; L14842; AAA53679.1; -; Genomic_DNA.
DR EMBL; AE005674; AAN43643.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP17472.1; -; Genomic_DNA.
DR PIR; S41534; S41534.
DR RefSeq; NP_707936.1; NC_004337.2.
DR RefSeq; WP_000699404.1; NZ_UIQL01000033.1.
DR AlphaFoldDB; P37777; -.
DR SMR; P37777; -.
DR STRING; 198214.SF2104; -.
DR PRIDE; P37777; -.
DR EnsemblBacteria; AAN43643; AAN43643; SF2104.
DR EnsemblBacteria; AAP17472; AAP17472; S2227.
DR GeneID; 1025931; -.
DR KEGG; sfl:SF2104; -.
DR KEGG; sft:NCTC1_02312; -.
DR KEGG; sfx:S2227; -.
DR PATRIC; fig|198214.7.peg.2512; -.
DR HOGENOM; CLU_007383_1_14_6; -.
DR OMA; EWCQHVQ; -.
DR OrthoDB; 707977at2; -.
DR UniPathway; UPA00124; -.
DR UniPathway; UPA00281; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; Chromosome.
DR GO; GO:0008460; F:dTDP-glucose 4,6-dehydratase activity; ISS:UniProtKB.
DR GO; GO:0019305; P:dTDP-rhamnose biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; ISS:UniProtKB.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; ISS:UniProtKB.
DR GO; GO:0009243; P:O antigen biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd05246; dTDP_GD_SDR_e; 1.
DR InterPro; IPR005888; dTDP_Gluc_deHydtase.
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.
DR TIGRFAMs; TIGR01181; dTDP_gluc_dehyt; 1.
PE 3: Inferred from homology;
KW Lipopolysaccharide biosynthesis; Lyase; NAD; Reference proteome.
FT CHAIN 1..361
FT /note="dTDP-glucose 4,6-dehydratase"
FT /id="PRO_0000183244"
FT ACT_SITE 134
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT ACT_SITE 135
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT ACT_SITE 167
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT BINDING 11..12
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT BINDING 32..35
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT BINDING 58..59
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT BINDING 80..84
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT BINDING 84
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26391"
FT BINDING 99
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT BINDING 133
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26391"
FT BINDING 167..171
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26391"
FT BINDING 197
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT BINDING 206..207
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26391"
FT BINDING 222..224
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26391"
FT BINDING 231
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26391"
FT BINDING 266
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26391"
FT BINDING 296..300
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26391"
FT CONFLICT 4
FT /note="L -> P (in Ref. 1; CAA50767)"
FT /evidence="ECO:0000305"
FT CONFLICT 70..76
FT /note="AQHQPDA -> RTAPARR (in Ref. 1; CAA50767)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="A -> T (in Ref. 1; CAA50767)"
FT /evidence="ECO:0000305"
FT CONFLICT 160..164
FT /note="AYAPS -> TKRQN (in Ref. 1; CAA50767)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="S -> N (in Ref. 1; CAA50767)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 361 AA; 40575 MW; CB880B2FF899F909 CRC64;
MKILVTGGAG FIGSAVVRHI INNTQDSVVN VDKLTYAGNL ESLADVSDSE RYAFEHADIC
DAVAMSRIFA QHQPDAVMHL AAESHVDRSI TGPAAFIETN IVGTYVLLEA ARNYWSALND
EKKKSFRFHH ISTDEVYGDL PHPDEANNNE ALPLFTETTA YAPSSPYSAS KASSDHLVRA
WKRTYGLPTI VTNCSNNYGP YHFPEKLIPL VILNALEGKA LPIYGKGDQI RDWLYVEDHA
RALYTVVTEG KAGETYNIGG HNEKKNIDVV LTICDLLDEI VPKEKSYREQ ITYVADRPGH
DRRYAIDADK ISRELGWKPQ ETFESGIRKT VEWYLANTNW VENVKSGTYQ SWIEQNYEGR
Q
