RMLB_NEIMA
ID RMLB_NEIMA Reviewed; 341 AA.
AC Q9S642; A1IP46;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 124.
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=NMA0189;
GN and
GN Name=rfbB2; OrderedLocusNames=NMA0204;
OS Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS Z2491).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122587;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MA-1 / Serogroup A;
RX PubMed=10024588; DOI=10.1128/iai.67.3.1405-1414.1999;
RA Lee F.K., Gibson B.W., Melaugh W., Zaleski A., Apicella M.A.;
RT "Relationship between UDP-glucose 4-epimerase activity and oligoglucose
RT glycoforms in two strains of Neisseria meningitidis.";
RL Infect. Immun. 67:1405-1414(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15465 / Z2491;
RX PubMed=10761919; DOI=10.1038/35006655;
RA Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA Barrell B.G.;
RT "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT Z2491.";
RL Nature 404:502-506(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}.
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DR EMBL; AF083467; AAD23919.1; -; Genomic_DNA.
DR EMBL; AL157959; CAM07504.1; -; Genomic_DNA.
DR EMBL; AL157959; CAM07518.1; -; Genomic_DNA.
DR PIR; G82014; G82014.
DR RefSeq; WP_002236574.1; NC_003116.1.
DR AlphaFoldDB; Q9S642; -.
DR SMR; Q9S642; -.
DR EnsemblBacteria; CAM07504; CAM07504; NMA0189.
DR EnsemblBacteria; CAM07518; CAM07518; NMA0204.
DR KEGG; nma:NMA0189; -.
DR KEGG; nma:NMA0204; -.
DR HOGENOM; CLU_007383_1_14_4; -.
DR OMA; FFTEDTP; -.
DR BioCyc; NMEN122587:NMA_RS00975-MON; -.
DR BioCyc; NMEN122587:NMA_RS01050-MON; -.
DR UniPathway; UPA00124; -.
DR UniPathway; UPA00281; -.
DR Proteomes; UP000000626; 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.
FT CHAIN 1..341
FT /note="dTDP-glucose 4,6-dehydratase"
FT /id="PRO_0000183241"
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"
SQ SEQUENCE 341 AA; 38224 MW; 826023B63916E72A CRC64;
MRKILVTGGA GFIGSAVVRH IIRNTQDSVV NLDKLTYAGN LESLTDIADN PRYAFEQVDI
CDRAELDRVF AQHRPDAVMH LAAESHVDRS IGSAGEFIQT NIVGTFNLLE AARAYRQQMP
SEKHEAFRFH HISTDEVYGD LSGTDDLFTE TAPYAPSSPY SASKASSDHL VRAWLRTYGL
PTIVTNCSNN YGPYHFPEKL IPLMILNALD GKPLPVYGDG MQIRDWLFVE DHARALYQVV
TEGVVGETYN IGGHNEKANI EVVKTICALL EELAPEKPAG VARYEDLITF VQDRPGHDAR
YAVDTAKIRR DLGWQPLETF ESGLRKTVQW YLDNKTRRQN A
