ID RMLB_NEIMB Reviewed; 355 AA. AC P55294; Q9JS14; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2001, sequence version 2. DT 28-JAN-2026, entry version 141. DE RecName: Full=dTDP-glucose 4,6-dehydratase {ECO:0000250|UniProtKB:P27830}; DE EC=4.2.1.46 {ECO:0000250|UniProtKB:P27830}; GN Name=rfbB1; OrderedLocusNames=NMB0063; GN and GN Name=rfbB2; OrderedLocusNames=NMB0079; OS Neisseria meningitidis serogroup B (strain ATCC BAA-335 / MC58). OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=B1940 / Serogroup B; RX PubMed=8022265; DOI=10.1111/j.1365-2958.1994.tb00367.x; RA Hammerschmidt S., Birkholz C., Zaehringer U., Robertson B.D., RA van Putten J.P.M., Ebeling O., Frosch M.; RT "Contribution of genes from the capsule gene complex (cps) to RT lipooligosaccharide biosynthesis and serum resistance in Neisseria RT meningitidis."; RL Mol. Microbiol. 11:885-896(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-335 / MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C., RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H., RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M., RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D., RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V., RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M., RA Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L09188; AAA63157.1; -; Genomic_DNA. DR EMBL; AE002098; AAF40531.1; -; Genomic_DNA. DR EMBL; AE002098; AAF40543.1; -; Genomic_DNA. DR PIR; G81242; G81242. DR PIR; S42431; S42431. DR RefSeq; WP_002224748.1; NC_003112.2. DR AlphaFoldDB; P55294; -. DR SMR; P55294; -. DR FunCoup; P55294; 347. DR STRING; 122586.NMB0063; -. DR PaxDb; 122586-NMB0063; -. DR KEGG; nme:NMB0063; -. DR KEGG; nme:NMB0079; -. DR PATRIC; fig|122586.8.peg.114; -. DR HOGENOM; CLU_007383_1_14_4; -. DR InParanoid; P55294; -. DR OrthoDB; 9803010at2; -. DR UniPathway; UPA00124; -. DR UniPathway; UPA00281; -. DR Proteomes; UP000000425; 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:0009103; P:lipopolysaccharide biosynthetic process; ISS:UniProtKB. DR GO; GO:0009243; P:O antigen biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0000271; P:polysaccharide biosynthetic process; ISS:UniProtKB. DR CDD; cd05246; dTDP_GD_SDR_e; 1. DR FunFam; 3.40.50.720:FF:000108; dTDP-glucose 4,6-dehydratase; 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; IPR005888; dTDP_Gluc_deHydtase. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR NCBIfam; TIGR01181; dTDP_gluc_dehyt; 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 3: Inferred from homology; KW Lipopolysaccharide biosynthesis; Lyase; NAD; Reference proteome. FT CHAIN 1..355 FT /note="dTDP-glucose 4,6-dehydratase" FT /id="PRO_0000183242" FT ACT_SITE 135 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:P27830" FT ACT_SITE 136 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P27830" FT ACT_SITE 160 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P27830" FT BINDING 12..13 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P27830" FT BINDING 33..36 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P27830" FT BINDING 59..60 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P27830" FT BINDING 81..85 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P27830" FT BINDING 85 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P26391" FT BINDING 100 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P27830" FT BINDING 134 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P26391" FT BINDING 160..164 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P27830" FT BINDING 189 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P26391" FT BINDING 190 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P27830" FT BINDING 199..200 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P26391" FT BINDING 215..217 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P26391" FT BINDING 224 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P26391" FT BINDING 259 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P26391" FT BINDING 293..297 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P26391" FT CONFLICT 1..3 FT /note="MRK -> MQTANKKT (in Ref. 1; AAA63157)" FT /evidence="ECO:0000305" FT CONFLICT 26..28 FT /note="RDA -> QDS (in Ref. 1; AAA63157)" FT /evidence="ECO:0000305" FT CONFLICT 32 FT /note="V -> L (in Ref. 1; AAA63157)" FT /evidence="ECO:0000305" FT CONFLICT 46..47 FT /note="EV -> DI (in Ref. 1; AAA63157)" FT /evidence="ECO:0000305" FT CONFLICT 73 FT /note="Y -> H (in Ref. 1; AAA63157)" FT /evidence="ECO:0000305" FT CONFLICT 142 FT /note="G -> H (in Ref. 1; AAA63157)" FT /evidence="ECO:0000305" FT CONFLICT 152 FT /note="A -> T (in Ref. 1; AAA63157)" FT /evidence="ECO:0000305" FT CONFLICT 268 FT /note="A -> T (in Ref. 1; AAA63157)" FT /evidence="ECO:0000305" FT CONFLICT 274 FT /note="A -> V (in Ref. 1; AAA63157)" FT /evidence="ECO:0000305" SQ SEQUENCE 355 AA; 39865 MW; 631AA0EDA02B6F41 CRC64; MRKILVTGGA GFIGSAVVRH IIRNTRDAVV NVDKLTYAGN LESLTEVADN PRYAFEQVDI CDRAELDRVF AQYRPDAVMH LAAESHVDRS IGSAGEFIQT NIVGTFNLLE AARAYWQQMP SEQHEAFRFH HISTDEVYGD LGGTDDLFTE TAPYAPSSPY SASKASSDHL VRAWLRTYGL PTIVTNCSNN YGPYHFPEKL IPLMILNALD GKPLPVYGDG MQIRDWLFVE DHARALYQVV TEGVVGETYN IGGHNEKANI EVVKTICALL EELAPEKPAG VARYEDLITF VQDRPGHDVR YAVDAAKIRR DLGWLPLETF ESGLRKTVQW YLDNKTWWQN VLNGSYRLER LGTGK //