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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)DescriptionActionsGraphical viewLength
Active sitei126Proton donorBy similarity1
Active sitei127Proton acceptorBy similarity1
Active sitei161Proton acceptorCurated1
Binding sitei190Substrate1 Publication1
Binding sitei225Substrate1 Publication1
Binding sitei260Substrate1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi11 – 17NAD1 Publication7
Nucleotide bindingi37 – 40NAD1 Publication4
Nucleotide bindingi62 – 63NAD1 Publication2
Nucleotide bindingi82 – 101NAD1 PublicationAdd BLAST20
Nucleotide bindingi161 – 191NAD1 PublicationAdd BLAST31

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

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)DescriptionActionsGraphical viewLength
ChainiPRO_00001832471 – 348dTDP-glucose 4,6-dehydrataseAdd BLAST348

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi210007.SMU_1457.

Structurei

Secondary structure

1348
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 10Combined sources6
Turni11 – 13Combined sources3
Helixi15 – 27Combined sources13
Beta strandi31 – 37Combined sources7
Helixi45 – 47Combined sources3
Helixi49 – 51Combined sources3
Beta strandi53 – 60Combined sources8
Helixi66 – 73Combined sources8
Beta strandi77 – 81Combined sources5
Helixi88 – 93Combined sources6
Helixi96 – 102Combined sources7
Helixi104 – 116Combined sources13
Beta strandi119 – 125Combined sources7
Helixi126 – 129Combined sources4
Helixi135 – 137Combined sources3
Turni139 – 142Combined sources4
Beta strandi147 – 149Combined sources3
Helixi160 – 179Combined sources20
Beta strandi183 – 188Combined sources6
Beta strandi191 – 193Combined sources3
Helixi201 – 211Combined sources11
Beta strandi216 – 218Combined sources3
Beta strandi224 – 226Combined sources3
Helixi230 – 243Combined sources14
Beta strandi249 – 252Combined sources4
Beta strandi257 – 259Combined sources3
Helixi260 – 270Combined sources11
Beta strandi278 – 281Combined sources4
Helixi296 – 302Combined sources7
Helixi311 – 324Combined sources14
Helixi326 – 329Combined sources4
Helixi330 – 332Combined sources3
Helixi333 – 341Combined sources9

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP95780.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni86 – 88Substrate binding3
Regioni125 – 127Substrate binding3
Regioni200 – 205Substrate binding6
Regioni216 – 218Substrate binding3
Regioni283 – 287Substrate binding5

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C1B. Bacteria.
COG1088. LUCA.
KOiK01710.
OMAiHNDNSLH.
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)DescriptionActionsGraphical viewLength
Sequence conflicti45R → H in BAA11249 (Ref. 1) Curated1
Sequence conflicti108I → T in BAA11249 (Ref. 1) Curated1
Sequence conflicti276N → D in BAA11249 (Ref. 1) Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KEPX-ray1.80A/B5-344[»]
1KETX-ray1.80A/B5-344[»]
ProteinModelPortaliP95780.
SMRiP95780.
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.
OMAiHNDNSLH.
PhylomeDBiP95780.

Enzyme and pathway databases

UniPathwayiUPA00124.

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...

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: November 2, 2016
This is version 123 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.