RMLB1_ECOLI
ID RMLB1_ECOLI Reviewed; 361 AA.
AC P37759; P78082;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=dTDP-glucose 4,6-dehydratase 1 {ECO:0000250|UniProtKB:P27830};
DE EC=4.2.1.46 {ECO:0000250|UniProtKB:P27830};
GN Name=rfbB; Synonyms=rmlB; OrderedLocusNames=b2041, JW2026;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / WG1;
RX PubMed=7517391; DOI=10.1128/jb.176.13.4144-4156.1994;
RA Stevenson G., Neal B., Liu D., Hobbs M., Packer N.H., Batley M.,
RA Redmond J.W., Lindquist L., Reeves P.R.;
RT "Structure of the O antigen of Escherichia coli K-12 and the sequence of
RT its rfb gene cluster.";
RL J. Bacteriol. 176:4144-4156(1994).
RN [2]
RP SEQUENCE REVISION TO 123 AND 250.
RC STRAIN=K12 / WG1;
RA Stevenson G.;
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP PATHWAY.
RX PubMed=7559340; DOI=10.1128/jb.177.19.5539-5546.1995;
RA Marolda C.L., Valvano M.A.;
RT "Genetic analysis of the dTDP-rhamnose biosynthesis region of the
RT Escherichia coli VW187 (O7:K1) rfb gene cluster: identification of
RT functional homologs of rfbB and rfbA in the rff cluster and correct
RT location of the rffE gene.";
RL J. Bacteriol. 177:5539-5546(1995).
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:0000269|PubMed:7559340}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC biosynthesis. {ECO:0000269|PubMed:7559340}.
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; U09876; AAB88398.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75102.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15883.1; -; Genomic_DNA.
DR PIR; H64969; H64969.
DR RefSeq; NP_416545.1; NC_000913.3.
DR RefSeq; WP_000699460.1; NZ_LN832404.1.
DR AlphaFoldDB; P37759; -.
DR SMR; P37759; -.
DR BioGRID; 4259679; 184.
DR BioGRID; 849655; 4.
DR DIP; DIP-10680N; -.
DR IntAct; P37759; 7.
DR STRING; 511145.b2041; -.
DR jPOST; P37759; -.
DR PaxDb; P37759; -.
DR PRIDE; P37759; -.
DR EnsemblBacteria; AAC75102; AAC75102; b2041.
DR EnsemblBacteria; BAA15883; BAA15883; BAA15883.
DR GeneID; 945276; -.
DR KEGG; ecj:JW2026; -.
DR KEGG; eco:b2041; -.
DR PATRIC; fig|1411691.4.peg.210; -.
DR EchoBASE; EB2311; -.
DR eggNOG; COG1088; Bacteria.
DR HOGENOM; CLU_007383_1_14_6; -.
DR InParanoid; P37759; -.
DR OMA; EWCQHVQ; -.
DR PhylomeDB; P37759; -.
DR BioCyc; EcoCyc:DTDPGLUCDEHYDRAT-MON; -.
DR BioCyc; MetaCyc:DTDPGLUCDEHYDRAT-MON; -.
DR SABIO-RK; P37759; -.
DR UniPathway; UPA00124; -.
DR UniPathway; UPA00281; -.
DR PRO; PR:P37759; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0008460; F:dTDP-glucose 4,6-dehydratase activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0051287; F:NAD binding; IDA:EcoCyc.
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:0009226; P:nucleotide-sugar biosynthetic process; IDA:EcoCyc.
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..361
FT /note="dTDP-glucose 4,6-dehydratase 1"
FT /id="PRO_0000183238"
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 296..300
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26391"
FT CONFLICT 123
FT /note="K -> E (in Ref. 1; AAB88398)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="G -> V (in Ref. 1; AAB88398)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 361 AA; 40558 MW; C3F64643271C14C7 CRC64;
MKILVTGGAG FIGSAVVRHI INNTQDSVVN VDKLTYAGNR ESLADVSDSE RYVFEHADIC
DAPAMARIFA QHQPDAVMHL AAESHVDRSI TGPAAFIETN IVGTYVLLEA ARNYWSALDS
DKKNSFRFHH ISTDEVYGDL PHPDEVNNTE ELPLFTETTA YAPSSPYSAS KASSDHLVRA
WKRTYGLPTI VTNCSNNYGP YHFPEKLIPL VILNALEGKA LPIYGKGDQI RDWLYVEDHA
RALYTVVTEG KAGETYNIGG HNEKKNIDVV LTICDLLDEI VPKEKSYREQ ITYVADRPGH
DRRYAIDAEK IGRALGWKPQ ETFESGIRKT VEWYLSNTKW VDNVKSGAYQ SWIEQNYEGR
Q
