RMLB_NEIGO
ID RMLB_NEIGO Reviewed; 346 AA.
AC P37761;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 96.
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 {ECO:0000303|PubMed:7961452};
OS Neisseria gonorrhoeae.
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=485;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MS11;
RX PubMed=7961452; DOI=10.1128/jb.176.22.6915-6920.1994;
RA Robertson B.D., Frosch M., van Putten J.P.M.;
RT "The identification of cryptic rhamnose biosynthesis genes in Neisseria
RT gonorrhoeae and their relationship to lipopolysaccharide biosynthesis.";
RL J. Bacteriol. 176:6915-6920(1994).
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; Z32742; CAA83652.1; -; Genomic_DNA.
DR EMBL; Z21508; CAA79718.1; -; Genomic_DNA.
DR PIR; S47045; S47045.
DR AlphaFoldDB; P37761; -.
DR SMR; P37761; -.
DR PRIDE; P37761; -.
DR UniPathway; UPA00124; -.
DR UniPathway; UPA00281; -.
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..346
FT /note="dTDP-glucose 4,6-dehydratase"
FT /id="PRO_0000183240"
FT ACT_SITE 140
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT ACT_SITE 141
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT ACT_SITE 165
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT BINDING 17..18
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT BINDING 38..41
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT BINDING 64..65
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT BINDING 86..90
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26391"
FT BINDING 105
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26391"
FT BINDING 165..169
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26391"
FT BINDING 195
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT BINDING 204..205
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26391"
FT BINDING 220..222
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26391"
FT BINDING 229
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26391"
FT BINDING 264
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26391"
FT BINDING 298..302
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26391"
SQ SEQUENCE 346 AA; 38829 MW; B52FD8125C567675 CRC64;
MQTEGKKNIL VTGGAGFIGS AVVRHIIQNT RDSVVNLDKL TYAGNLESLT DIADNPRYAF
EQVDICDRAE LDRVFAQYRP DAVMHLAAES HVDRAIGSAG EFIRTNIVGT FDLLEAARAY
WQQMPSEKRE AFRFHHISTD EVYGDLHGTD DLFTETTPYA PSSPYSASKA AADHLVRAWQ
RTYRLPSIVS NCSNNYGPRQ FPEKLIPLMI LNALSGKPLP VYGDGAQIRD WLFVEDHARA
LYQVVTEGVV GETYNIGGHN EKTNLEVVKT ICALLEELAP EKPAGVARYE DLITFVQDRP
GHDARYAVDA AKIRRDLGWL PLETFESGLR KTVQWYLDNK TRRQNA
