RMLB2_ECOLI
ID RMLB2_ECOLI Reviewed; 355 AA.
AC P27830; P76754; Q2M896; Q6BF01;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 3.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=dTDP-glucose 4,6-dehydratase 2 {ECO:0000303|PubMed:7559340};
DE EC=4.2.1.46 {ECO:0000269|PubMed:11380254, ECO:0000269|PubMed:11601973, ECO:0000269|PubMed:7559340};
GN Name=rffG; OrderedLocusNames=b3788, JW5598;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=1379743; DOI=10.1126/science.1379743;
RA Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.;
RT "Analysis of the Escherichia coli genome: DNA sequence of the region from
RT 84.5 to 86.5 minutes.";
RL Science 257:771-778(1992).
RN [2]
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 [3]
RP SEQUENCE REVISION TO 314-315.
RX PubMed=16397293; DOI=10.1093/nar/gkj405;
RA Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R.,
RA Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T.,
RA Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H.,
RA Thomson N.R., Wishart D., Wanner B.L.;
RT "Escherichia coli K-12: a cooperatively developed annotation snapshot
RT -- 2005.";
RL Nucleic Acids Res. 34:1-9(2006).
RN [4]
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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND 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).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVE SITES.
RX PubMed=11380254; DOI=10.1021/bi010441a;
RA Hegeman A.D., Gross J.W., Frey P.A.;
RT "Probing catalysis by Escherichia coli dTDP-glucose-4,6-dehydratase:
RT identification and preliminary characterization of functional amino acid
RT residues at the active site.";
RL Biochemistry 40:6598-6610(2001).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVE SITES.
RX PubMed=11601973; DOI=10.1021/bi011138c;
RA Gross J.W., Hegeman A.D., Gerratana B., Frey P.A.;
RT "Dehydration is catalyzed by glutamate-136 and aspartic acid-135 active
RT site residues in Escherichia coli dTDP-glucose 4,6-dehydratase.";
RL Biochemistry 40:12497-12504(2001).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH NAD, COFACTOR, AND
RP SUBUNIT.
RA Thoden J.B., Hegeman A.D., Frey P.A., Holden H.M.;
RT "Molecular structure of dTDP-glucose 4,6-dehydratase from E. coli.";
RL Submitted (OCT-1998) to the PDB data bank.
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:0000269|PubMed:11380254,
CC ECO:0000269|PubMed:11601973, ECO:0000269|PubMed:7559340}.
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:11380254, ECO:0000269|PubMed:11601973,
CC ECO:0000269|PubMed:7559340};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000269|Ref.8};
CC Note=Binds 1 NAD(+) per subunit. {ECO:0000269|Ref.8};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; dTDP-4-acetamido-4,6-
CC dideoxygalactose biosynthesis. {ECO:0000269|PubMed:7559340}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; enterobacterial common
CC antigen biosynthesis. {ECO:0000269|PubMed:7559340}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|Ref.8}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. dTDP-glucose dehydratase subfamily. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be rffE, the UDP-N-acetylglucosamine
CC epimerase. {ECO:0000305|PubMed:1379743}.
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DR EMBL; M87049; AAA67588.1; -; Genomic_DNA.
DR EMBL; U00096; AAT48213.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77510.1; -; Genomic_DNA.
DR PIR; G65182; G65182.
DR RefSeq; WP_001226601.1; NZ_SSZK01000025.1.
DR RefSeq; YP_026255.1; NC_000913.3.
DR PDB; 1BXK; X-ray; 1.90 A; A/B=1-355.
DR PDBsum; 1BXK; -.
DR AlphaFoldDB; P27830; -.
DR SMR; P27830; -.
DR BioGRID; 4262077; 235.
DR STRING; 511145.b3788; -.
DR jPOST; P27830; -.
DR PaxDb; P27830; -.
DR PRIDE; P27830; -.
DR EnsemblBacteria; AAT48213; AAT48213; b3788.
DR EnsemblBacteria; BAE77510; BAE77510; BAE77510.
DR GeneID; 948300; -.
DR KEGG; ecj:JW5598; -.
DR KEGG; eco:b3788; -.
DR PATRIC; fig|511145.12.peg.3904; -.
DR EchoBASE; EB1422; -.
DR eggNOG; COG1088; Bacteria.
DR HOGENOM; CLU_007383_1_14_6; -.
DR InParanoid; P27830; -.
DR OMA; KLIPLMC; -.
DR PhylomeDB; P27830; -.
DR BioCyc; EcoCyc:DTDPGLUCDEHYDRAT2-MON; -.
DR BioCyc; MetaCyc:DTDPGLUCDEHYDRAT2-MON; -.
DR BRENDA; 4.2.1.46; 2026.
DR SABIO-RK; P27830; -.
DR UniPathway; UPA00566; -.
DR UniPathway; UPA00817; -.
DR EvolutionaryTrace; P27830; -.
DR PRO; PR:P27830; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0008460; F:dTDP-glucose 4,6-dehydratase activity; IDA:UniProtKB.
DR GO; GO:0009246; P:enterobacterial common antigen biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009225; P:nucleotide-sugar metabolic process; IEA:InterPro.
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 3D-structure; Lyase; NAD; Reference proteome.
FT CHAIN 1..355
FT /note="dTDP-glucose 4,6-dehydratase 2"
FT /id="PRO_0000183236"
FT ACT_SITE 135
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:11380254,
FT ECO:0000269|PubMed:11601973"
FT ACT_SITE 136
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:11380254,
FT ECO:0000269|PubMed:11601973"
FT ACT_SITE 160
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:11380254,
FT ECO:0000269|PubMed:11601973"
FT BINDING 12..13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PDB:1BXK"
FT BINDING 33..36
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PDB:1BXK"
FT BINDING 59..60
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PDB:1BXK"
FT BINDING 81..85
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000305|Ref.8, ECO:0007744|PDB:1BXK"
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:0000269|Ref.8, ECO:0007744|PDB:1BXK"
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:0000269|Ref.8, ECO:0007744|PDB:1BXK"
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:0000269|Ref.8, ECO:0007744|PDB:1BXK"
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 314..315
FT /note="WL -> CV (in Ref. 1; AAA67588)"
FT /evidence="ECO:0000305"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:1BXK"
FT TURN 8..10
FT /evidence="ECO:0007829|PDB:1BXK"
FT HELIX 12..24
FT /evidence="ECO:0007829|PDB:1BXK"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:1BXK"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:1BXK"
FT TURN 44..49
FT /evidence="ECO:0007829|PDB:1BXK"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:1BXK"
FT HELIX 63..73
FT /evidence="ECO:0007829|PDB:1BXK"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:1BXK"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:1BXK"
FT HELIX 96..101
FT /evidence="ECO:0007829|PDB:1BXK"
FT HELIX 103..117
FT /evidence="ECO:0007829|PDB:1BXK"
FT HELIX 121..126
FT /evidence="ECO:0007829|PDB:1BXK"
FT STRAND 128..134
FT /evidence="ECO:0007829|PDB:1BXK"
FT HELIX 135..138
FT /evidence="ECO:0007829|PDB:1BXK"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:1BXK"
FT HELIX 159..178
FT /evidence="ECO:0007829|PDB:1BXK"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:1BXK"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:1BXK"
FT HELIX 200..209
FT /evidence="ECO:0007829|PDB:1BXK"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:1BXK"
FT HELIX 229..242
FT /evidence="ECO:0007829|PDB:1BXK"
FT STRAND 248..251
FT /evidence="ECO:0007829|PDB:1BXK"
FT HELIX 259..273
FT /evidence="ECO:0007829|PDB:1BXK"
FT HELIX 284..287
FT /evidence="ECO:0007829|PDB:1BXK"
FT HELIX 306..311
FT /evidence="ECO:0007829|PDB:1BXK"
FT HELIX 320..333
FT /evidence="ECO:0007829|PDB:1BXK"
FT HELIX 335..343
FT /evidence="ECO:0007829|PDB:1BXK"
FT HELIX 345..348
FT /evidence="ECO:0007829|PDB:1BXK"
SQ SEQUENCE 355 AA; 39754 MW; 34DBD1EFB42DB9B3 CRC64;
MRKILITGGA GFIGSALVRY IINETSDAVV VVDKLTYAGN LMSLAPVAQS ERFAFEKVDI
CDRAELARVF TEHQPDCVMH LAAESHVDRS IDGPAAFIET NIVGTYTLLE AARAYWNALT
EDKKSAFRFH HISTDEVYGD LHSTDDFFTE TTPYAPSSPY SASKASSDHL VRAWLRTYGL
PTLITNCSNN YGPYHFPEKL IPLMILNALA GKSLPVYGNG QQIRDWLYVE DHARALYCVA
TTGKVGETYN IGGHNERKNL DVVETICELL EELAPNKPHG VAHYRDLITF VADRPGHDLR
YAIDASKIAR ELGWLPQETF ESGMRKTVQW YLANESWWKQ VQDGSYQGER LGLKG
