RMLB2_ECOLX
ID RMLB2_ECOLX Reviewed; 362 AA.
AC Q6E7F4;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=dTDP-glucose 4,6-dehydratase {ECO:0000303|PubMed:19019146};
DE EC=4.2.1.46 {ECO:0000269|PubMed:19019146};
GN Name=rmlB;
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=O52 / G1066;
RX PubMed=15231783; DOI=10.1128/jb.186.14.4510-4519.2004;
RA Feng L., Senchenkova S.N., Yang J., Shashkov A.S., Tao J., Guo H.,
RA Cheng J., Ren Y., Knirel Y.A., Reeves P.R., Wang L.;
RT "Synthesis of the heteropolysaccharide O antigen of Escherichia coli O52
RT requires an ABC transporter: structural and genetic evidence.";
RL J. Bacteriol. 186:4510-4519(2004).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=O52 / G1066;
RX PubMed=19019146; DOI=10.1111/j.1365-2958.2008.06449.x;
RA Wang Q., Ding P., Perepelov A.V., Xu Y., Wang Y., Knirel Y.A., Wang L.,
RA Feng L.;
RT "Characterization of the dTDP-D-fucofuranose biosynthetic pathway in
RT Escherichia coli O52.";
RL Mol. Microbiol. 70:1358-1367(2008).
CC -!- FUNCTION: Catalyzes the dehydration of dTDP-D-glucose to form dTDP-4-
CC dehydro-6-deoxy-D-glucose via a three-step process involving oxidation,
CC dehydration and reduction. This reaction is a step in the biosynthesis
CC of D-fucofuranose, a component of E.coli O52 O antigen.
CC {ECO:0000269|PubMed:19019146}.
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:0000269|PubMed:19019146};
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: Bacterial outer membrane biogenesis; LPS O-antigen
CC biosynthesis. {ECO:0000269|PubMed:19019146}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. dTDP-glucose dehydratase subfamily. {ECO:0000305}.
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DR EMBL; AY528413; AAS99159.1; -; Genomic_DNA.
DR RefSeq; WP_001575913.1; NZ_UIHN01000014.1.
DR AlphaFoldDB; Q6E7F4; -.
DR SMR; Q6E7F4; -.
DR BioCyc; MetaCyc:MON-18133; -.
DR UniPathway; UPA00281; -.
DR GO; GO:0008460; F:dTDP-glucose 4,6-dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0009225; P:nucleotide-sugar metabolic process; IEA:InterPro.
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 1: Evidence at protein level;
KW Carbohydrate metabolism; Lipopolysaccharide biosynthesis; Lyase; NAD.
FT CHAIN 1..362
FT /note="dTDP-glucose 4,6-dehydratase"
FT /id="PRO_0000425108"
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 300..304
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26391"
SQ SEQUENCE 362 AA; 40886 MW; 9B9D0F8FAD829C49 CRC64;
MKILVTGGAG FIGSAVVRHI INNTQDSVIN VDKLTYAGNL ESLTEIENNE RYKFEHADIC
DSVAIANIFA HHQPDAIMHL AAESHVDRSI TGPADFIETN IVGTYILLEE ARKYWLALSE
DRKGAFRFHH ISTDEVYGDL PHPDEVSSDT ILPLFTEQTS YSPSSPYSAS KASSDHLVRA
WRRTYGLPTI VTNCSNNYGP YHFPEKLIPL IILNAIAGKL LPVYGNGEQI RDWLYVEDHA
RALYEVVTKG VPGETYNIGG HNERKNIDVV KTICRILDEL IADKPDGIEN FEQLIRYVSD
RPGHDLRYAI DASKIKQDLG WVPQETFETG ITKTIHWYLN NKEWWQRVMD GSYAGERLGL
VE
