RMLB_NEIMB
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 03-AUG-2022, entry version 125.
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 MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC 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=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; NP_273127.1; NC_003112.2.
DR RefSeq; NP_273142.1; NC_003112.2.
DR RefSeq; WP_002224748.1; NC_003112.2.
DR AlphaFoldDB; P55294; -.
DR SMR; P55294; -.
DR STRING; 122586.NMB0063; -.
DR PaxDb; P55294; -.
DR EnsemblBacteria; AAF40531; AAF40531; NMB0063.
DR EnsemblBacteria; AAF40543; AAF40543; NMB0079.
DR KEGG; nme:NMB0063; -.
DR KEGG; nme:NMB0079; -.
DR PATRIC; fig|122586.8.peg.114; -.
DR HOGENOM; CLU_007383_1_14_4; -.
DR OMA; FFTEDTP; -.
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: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..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
