Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

dTDP-glucose 4,6-dehydratase

Gene

rmlB

Organism
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the dehydration of dTDP-D-glucose to form dTDP-6-deoxy-D-xylo-4-hexulose via a three-step process involving oxidation, dehydration and reduction.By similarity

Catalytic activityi

dTDP-alpha-D-glucose = dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O.

Cofactori

NAD+1 PublicationNote: Binds 1 NAD+ per subunit.1 Publication

Pathwayi: dTDP-L-rhamnose biosynthesis

This protein is involved in the pathway dTDP-L-rhamnose biosynthesis, which is part of Carbohydrate biosynthesis.
View all proteins of this organism that are known to be involved in the pathway dTDP-L-rhamnose biosynthesis and in Carbohydrate biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei126 – 1261Proton donorBy similarity
Active sitei127 – 1271Proton acceptorBy similarity
Active sitei161 – 1611Proton acceptorCurated
Binding sitei190 – 1901Substrate1 Publication
Binding sitei225 – 2251Substrate1 Publication
Binding sitei260 – 2601Substrate1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi11 – 177NAD1 Publication
Nucleotide bindingi37 – 404NAD1 Publication
Nucleotide bindingi62 – 632NAD1 Publication
Nucleotide bindingi82 – 10120NAD1 PublicationAdd
BLAST
Nucleotide bindingi161 – 19131NAD1 PublicationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Lipopolysaccharide biosynthesis

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciSMUT210007:GC7Z-1371-MONOMER.
UniPathwayiUPA00124.

Names & Taxonomyi

Protein namesi
Recommended name:
dTDP-glucose 4,6-dehydratase (EC:4.2.1.46)
Gene namesi
Name:rmlB
Ordered Locus Names:SMU_1457
OrganismiStreptococcus mutans serotype c (strain ATCC 700610 / UA159)
Taxonomic identifieri210007 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
Proteomesi
  • UP000002512 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 348348dTDP-glucose 4,6-dehydratasePRO_0000183247Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi210007.SMU_1457.

Structurei

Secondary structure

1
348
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 106Combined sources
Turni11 – 133Combined sources
Helixi15 – 2713Combined sources
Beta strandi31 – 377Combined sources
Helixi45 – 473Combined sources
Helixi49 – 513Combined sources
Beta strandi53 – 608Combined sources
Helixi66 – 738Combined sources
Beta strandi77 – 815Combined sources
Helixi88 – 936Combined sources
Helixi96 – 1027Combined sources
Helixi104 – 11613Combined sources
Beta strandi119 – 1257Combined sources
Helixi126 – 1294Combined sources
Helixi135 – 1373Combined sources
Turni139 – 1424Combined sources
Beta strandi147 – 1493Combined sources
Helixi160 – 17920Combined sources
Beta strandi183 – 1886Combined sources
Beta strandi191 – 1933Combined sources
Helixi201 – 21111Combined sources
Beta strandi216 – 2183Combined sources
Beta strandi224 – 2263Combined sources
Helixi230 – 24314Combined sources
Beta strandi249 – 2524Combined sources
Beta strandi257 – 2593Combined sources
Helixi260 – 27011Combined sources
Beta strandi278 – 2814Combined sources
Helixi296 – 3027Combined sources
Helixi311 – 32414Combined sources
Helixi326 – 3294Combined sources
Helixi330 – 3323Combined sources
Helixi333 – 3419Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KEPX-ray1.80A/B5-344[»]
1KETX-ray1.80A/B5-344[»]
ProteinModelPortaliP95780.
SMRiP95780. Positions 3-347.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP95780.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni86 – 883Substrate binding
Regioni125 – 1273Substrate binding
Regioni200 – 2056Substrate binding
Regioni216 – 2183Substrate binding
Regioni283 – 2875Substrate binding

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C1B. Bacteria.
COG1088. LUCA.
KOiK01710.
OMAiHEDWWKA.
OrthoDBiEOG6PZXCX.
PhylomeDBiP95780.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR005888. dTDP_Gluc_deHydtase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF16363. GDP_Man_Dehyd. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01181. dTDP_gluc_dehyt. 1 hit.

Sequencei

Sequence statusi: Complete.

P95780-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTEYKNIIVT GGAGFIGSNF VHYVYNNHPD VHVTVLDKLT YAGNRANLEE
60 70 80 90 100
ILGDRVELVV GDIADSELVD KLAAKADAIV HYAAESHNDN SLKDPSPFIY
110 120 130 140 150
TNFVGTYILL EAARKYDIRF HHVSTDEVYG DLPLREDLPG HGEGPGEKFT
160 170 180 190 200
AETKYNPSSP YSSTKAASDL IVKAWVRSFG VKATISNCSN NYGPYQHIEK
210 220 230 240 250
FIPRQITNIL SGIKPKLYGE GKNVRDWIHT NDHSTGVWAI LTKGRIGETY
260 270 280 290 300
LIGADGEKNN KEVLELILEK MSQPKNAYDH VTDRAGHDLR YAIDSTKLRE
310 320 330 340
ELGWKPQFTN FEEGLEDTIK WYTEHEDWWK AEKEAVEANY AKTQKILN
Length:348
Mass (Da):39,281
Last modified:November 28, 2002 - v2
Checksum:i9DBDEA3CACF27216
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti45 – 451R → H in BAA11249 (Ref. 1) Curated
Sequence conflicti108 – 1081I → T in BAA11249 (Ref. 1) Curated
Sequence conflicti276 – 2761N → D in BAA11249 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D78182 Genomic DNA. Translation: BAA11249.1.
AE014133 Genomic DNA. Translation: AAN59116.1.
RefSeqiNP_721810.1. NC_004350.2.
WP_002263087.1. NC_004350.2.

Genome annotation databases

EnsemblBacteriaiAAN59116; AAN59116; SMU_1457.
GeneIDi1028708.
KEGGismu:SMU_1457.
PATRICi19664935. VBIStrMut61772_1296.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D78182 Genomic DNA. Translation: BAA11249.1.
AE014133 Genomic DNA. Translation: AAN59116.1.
RefSeqiNP_721810.1. NC_004350.2.
WP_002263087.1. NC_004350.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KEPX-ray1.80A/B5-344[»]
1KETX-ray1.80A/B5-344[»]
ProteinModelPortaliP95780.
SMRiP95780. Positions 3-347.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi210007.SMU_1457.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAN59116; AAN59116; SMU_1457.
GeneIDi1028708.
KEGGismu:SMU_1457.
PATRICi19664935. VBIStrMut61772_1296.

Phylogenomic databases

eggNOGiENOG4105C1B. Bacteria.
COG1088. LUCA.
KOiK01710.
OMAiHEDWWKA.
OrthoDBiEOG6PZXCX.
PhylomeDBiP95780.

Enzyme and pathway databases

UniPathwayiUPA00124.
BioCyciSMUT210007:GC7Z-1371-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP95780.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR005888. dTDP_Gluc_deHydtase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF16363. GDP_Man_Dehyd. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01181. dTDP_gluc_dehyt. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Tsukioka Y., Yamashita Y., Nakano Y., Oho T., Koga T.
    Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: XC.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700610 / UA159.
  3. Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 5-344 IN COMPLEX WITH SUBSTRATE AND NAD, COFACTOR, SUBUNIT.

Entry informationi

Entry nameiRMLB_STRMU
AccessioniPrimary (citable) accession number: P95780
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 28, 2002
Last modified: December 9, 2015
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.