RMLB_STRMU
ID RMLB_STRMU Reviewed; 348 AA.
AC P95780;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=dTDP-glucose 4,6-dehydratase {ECO:0000250|UniProtKB:P27830};
DE EC=4.2.1.46 {ECO:0000250|UniProtKB:P27830};
GN Name=rmlB; OrderedLocusNames=SMU_1457;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=XC;
RA Tsukioka Y., Yamashita Y., Nakano Y., Oho T., Koga T.;
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 5-344 IN COMPLEX WITH SUBSTRATE
RP AND NAD, COFACTOR, AND SUBUNIT.
RX PubMed=11796113; DOI=10.1016/s0969-2126(01)00694-3;
RA Allard S.T., Beis K., Giraud M.-F., Hegeman A.D., Gross J.W.,
RA Wilmouth R.C., Whitfield C., Graninger M., Messner P., Allen A.G.,
RA Maskell D.J., Naismith J.H.;
RT "Toward a structural understanding of the dehydratase mechanism.";
RL Structure 10:81-92(2002).
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:0000269|PubMed:11796113};
CC Note=Binds 1 NAD(+) per subunit. {ECO:0000269|PubMed:11796113};
CC -!- PATHWAY: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
CC {ECO:0000250|UniProtKB:P37759}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11796113}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. dTDP-glucose dehydratase subfamily. {ECO:0000305}.
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DR EMBL; D78182; BAA11249.1; -; Genomic_DNA.
DR EMBL; AE014133; AAN59116.1; -; Genomic_DNA.
DR RefSeq; NP_721810.1; NC_004350.2.
DR RefSeq; WP_002263087.1; NC_004350.2.
DR PDB; 1KEP; X-ray; 1.80 A; A/B=5-344.
DR PDB; 1KET; X-ray; 1.80 A; A/B=5-344.
DR PDBsum; 1KEP; -.
DR PDBsum; 1KET; -.
DR AlphaFoldDB; P95780; -.
DR SMR; P95780; -.
DR STRING; 210007.SMU_1457; -.
DR DrugBank; DB03751; 2'deoxy-Thymidine-5'-Diphospho-Alpha-D-Glucose.
DR DrugBank; DB03161; Thymidine-5'-diphospho-beta-D-xylose.
DR PRIDE; P95780; -.
DR EnsemblBacteria; AAN59116; AAN59116; SMU_1457.
DR KEGG; smu:SMU_1457; -.
DR PATRIC; fig|210007.7.peg.1296; -.
DR eggNOG; COG1088; Bacteria.
DR HOGENOM; CLU_007383_1_14_9; -.
DR OMA; KLIPLMC; -.
DR PhylomeDB; P95780; -.
DR UniPathway; UPA00124; -.
DR EvolutionaryTrace; P95780; -.
DR Proteomes; UP000002512; 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; IEA:UniProtKB-KW.
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; Lipopolysaccharide biosynthesis; Lyase; NAD;
KW Reference proteome.
FT CHAIN 1..348
FT /note="dTDP-glucose 4,6-dehydratase"
FT /id="PRO_0000183247"
FT ACT_SITE 126
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT ACT_SITE 127
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT ACT_SITE 161
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:11796113,
FT ECO:0007744|PDB:1KEP, ECO:0007744|PDB:1KET"
FT BINDING 15..16
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:11796113,
FT ECO:0007744|PDB:1KEP, ECO:0007744|PDB:1KET"
FT BINDING 37..40
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:11796113,
FT ECO:0007744|PDB:1KEP, ECO:0007744|PDB:1KET"
FT BINDING 62..63
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:11796113,
FT ECO:0007744|PDB:1KEP, ECO:0007744|PDB:1KET"
FT BINDING 82..86
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:11796113,
FT ECO:0007744|PDB:1KEP, ECO:0007744|PDB:1KET"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26391"
FT BINDING 88
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11796113,
FT ECO:0007744|PDB:1KET"
FT BINDING 101
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:11796113,
FT ECO:0007744|PDB:1KEP, ECO:0007744|PDB:1KET"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11796113,
FT ECO:0007744|PDB:1KEP"
FT BINDING 161..165
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000305|PubMed:11796113,
FT ECO:0007744|PDB:1KEP, ECO:0007744|PDB:1KET"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11796113,
FT ECO:0007744|PDB:1KET"
FT BINDING 191
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:11796113,
FT ECO:0007744|PDB:1KEP, ECO:0007744|PDB:1KET"
FT BINDING 200..205
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11796113,
FT ECO:0007744|PDB:1KEP, ECO:0007744|PDB:1KET"
FT BINDING 216..218
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11796113,
FT ECO:0007744|PDB:1KET"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11796113,
FT ECO:0007744|PDB:1KET"
FT BINDING 260
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11796113,
FT ECO:0007744|PDB:1KET"
FT BINDING 283..287
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:11796113,
FT ECO:0007744|PDB:1KET"
FT CONFLICT 45
FT /note="R -> H (in Ref. 1; BAA11249)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="I -> T (in Ref. 1; BAA11249)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="N -> D (in Ref. 1; BAA11249)"
FT /evidence="ECO:0000305"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:1KET"
FT TURN 11..13
FT /evidence="ECO:0007829|PDB:1KET"
FT HELIX 15..27
FT /evidence="ECO:0007829|PDB:1KET"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:1KET"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:1KET"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:1KET"
FT STRAND 53..60
FT /evidence="ECO:0007829|PDB:1KET"
FT HELIX 66..73
FT /evidence="ECO:0007829|PDB:1KET"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:1KET"
FT HELIX 88..93
FT /evidence="ECO:0007829|PDB:1KET"
FT HELIX 96..102
FT /evidence="ECO:0007829|PDB:1KET"
FT HELIX 104..116
FT /evidence="ECO:0007829|PDB:1KET"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:1KET"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:1KET"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:1KET"
FT TURN 139..142
FT /evidence="ECO:0007829|PDB:1KET"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:1KET"
FT HELIX 160..179
FT /evidence="ECO:0007829|PDB:1KET"
FT STRAND 183..188
FT /evidence="ECO:0007829|PDB:1KET"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:1KET"
FT HELIX 201..210
FT /evidence="ECO:0007829|PDB:1KET"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:1KET"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:1KET"
FT HELIX 230..243
FT /evidence="ECO:0007829|PDB:1KET"
FT STRAND 249..252
FT /evidence="ECO:0007829|PDB:1KET"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:1KET"
FT HELIX 260..270
FT /evidence="ECO:0007829|PDB:1KET"
FT STRAND 278..281
FT /evidence="ECO:0007829|PDB:1KET"
FT HELIX 296..302
FT /evidence="ECO:0007829|PDB:1KET"
FT HELIX 311..324
FT /evidence="ECO:0007829|PDB:1KET"
FT HELIX 326..328
FT /evidence="ECO:0007829|PDB:1KET"
FT TURN 329..332
FT /evidence="ECO:0007829|PDB:1KET"
FT HELIX 333..341
FT /evidence="ECO:0007829|PDB:1KET"
SQ SEQUENCE 348 AA; 39281 MW; 9DBDEA3CACF27216 CRC64;
MTEYKNIIVT GGAGFIGSNF VHYVYNNHPD VHVTVLDKLT YAGNRANLEE ILGDRVELVV
GDIADSELVD KLAAKADAIV HYAAESHNDN SLKDPSPFIY TNFVGTYILL EAARKYDIRF
HHVSTDEVYG DLPLREDLPG HGEGPGEKFT AETKYNPSSP YSSTKAASDL IVKAWVRSFG
VKATISNCSN NYGPYQHIEK FIPRQITNIL SGIKPKLYGE GKNVRDWIHT NDHSTGVWAI
LTKGRIGETY LIGADGEKNN KEVLELILEK MSQPKNAYDH VTDRAGHDLR YAIDSTKLRE
ELGWKPQFTN FEEGLEDTIK WYTEHEDWWK AEKEAVEANY AKTQKILN
