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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: -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.By similarity

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.By similarity
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
Binding sitei86Substrate; via carbonyl oxygenBy similarity1
Binding sitei88SubstrateCombined sources1 Publication1
Binding sitei101NADCombined sources1 Publication1
Binding sitei125SubstrateCombined sources1 Publication1
Active sitei126Proton donorBy similarity1
Active sitei127Proton acceptorBy similarity1
Active sitei161Proton acceptorCombined sources1 Publication1
Binding sitei190SubstrateCombined sources1 Publication1
Binding sitei191NADCombined sources1 Publication1
Binding sitei225SubstrateCombined sources1 Publication1
Binding sitei260SubstrateCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi15 – 16NADCombined sources1 Publication2
Nucleotide bindingi37 – 40NADCombined sources1 Publication4
Nucleotide bindingi62 – 63NADCombined sources1 Publication2
Nucleotide bindingi82 – 86NADCombined sources1 Publication5
Nucleotide bindingi161 – 165NADCombined sources1 Publication5

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLyase
Biological processLipopolysaccharide biosynthesis
LigandNAD

Enzyme and pathway databases

BioCyciSMUT210007:G1FZX-1370-MONOMER
UniPathwayiUPA00124

Names & Taxonomyi

Protein namesi
Recommended name:
dTDP-glucose 4,6-dehydrataseBy similarity (EC:4.2.1.46By similarity)
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

Pathology & Biotechi

Chemistry databases

DrugBankiDB03751 2'deoxy-Thymidine-5'-Diphospho-Alpha-D-Glucose
DB03161 Thymidine-5'-Diphospho-Beta-D-Xylose

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 strandi32 – 37Combined sources6
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 – 210Combined sources10
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 – 328Combined sources3
Turni329 – 332Combined sources4
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
Regioni200 – 205Substrate bindingCombined sources1 Publication6
Regioni216 – 218Substrate bindingCombined sources1 Publication3
Regioni283 – 287Substrate bindingCombined sources1 Publication5

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C1B Bacteria
COG1088 LUCA
KOiK01710
OMAiKLIPLMC
PhylomeDBiP95780

Family and domain databases

InterProiView protein in InterPro
IPR005888 dTDP_Gluc_deHydtase
IPR016040 NAD(P)-bd_dom
IPR036291 NAD(P)-bd_dom_sf
PfamiView protein in Pfam
PF16363 GDP_Man_Dehyd, 1 hit
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
PATRICifig|210007.7.peg.1296

Similar proteinsi

Entry informationi

Entry nameiRMLB_STRMU
AccessioniPrimary (citable) accession number: P95780
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 28, 2002
Last modified: May 23, 2018
This is version 130 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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