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Protein

dTDP-glucose 4,6-dehydratase

Gene

rfbB

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
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.1 Publication

Catalytic activityi

dTDP-alpha-D-glucose = dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O.1 Publication

Cofactori

NAD+2 PublicationsNote: Binds 1 NAD+ per subunit.2 Publications

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.

Pathwayi: LPS O-antigen biosynthesis

This protein is involved in the pathway LPS O-antigen biosynthesis, which is part of Bacterial outer membrane biogenesis.By similarity
View all proteins of this organism that are known to be involved in the pathway LPS O-antigen biosynthesis and in Bacterial outer membrane biogenesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei84Substrate; via carbonyl oxygenCombined sources1 Publication1
Binding sitei99NADCombined sources2 Publications1
Binding sitei133SubstrateCombined sources1 Publication1
Active sitei134Proton donorCombined sources1 Publication1
Active sitei135Proton acceptorBy similarity1
Active sitei167Proton acceptorCombined sources1 Publication1
Binding sitei196SubstrateCombined sources1 Publication1
Binding sitei197NAD; via amide nitrogenCombined sources2 Publications1
Binding sitei231SubstrateCombined sources1 Publication1
Binding sitei266SubstrateCombined sources1 Publication1
Binding sitei357SubstrateCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi11 – 12NADCombined sources2 Publications2
Nucleotide bindingi32 – 35NADCombined sources2 Publications4
Nucleotide bindingi58 – 59NADCombined sources2 Publications2
Nucleotide bindingi80 – 84NADCombined sources1 Publication1 Publication5
Nucleotide bindingi167 – 171NADCombined sources2 Publications5

GO - Molecular functioni

  • dTDP-glucose 4,6-dehydratase activity Source: UniProtKB
  • NADH binding Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionLyase
Biological processLipopolysaccharide biosynthesis
LigandNAD

Enzyme and pathway databases

BioCyciSENT99287:G1FZD-2116-MONOMER
SABIO-RKiP26391
UniPathwayiUPA00124
UPA00281

Names & Taxonomyi

Protein namesi
Recommended name:
dTDP-glucose 4,6-dehydratase1 Publication (EC:4.2.1.461 Publication)
Gene namesi
Name:rfbB1 Publication
Ordered Locus Names:STM2097
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeSalmonella
Proteomesi
  • UP000001014 Componenti: Chromosome

Pathology & Biotechi

Chemistry databases

DrugBankiDB03751 2'deoxy-Thymidine-5'-Diphospho-Alpha-D-Glucose

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001832431 – 361dTDP-glucose 4,6-dehydrataseAdd BLAST361

Proteomic databases

PaxDbiP26391
PRIDEiP26391

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

STRINGi99287.STM2097

Structurei

Secondary structure

1361
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 7Combined sources6
Helixi11 – 23Combined sources13
Beta strandi27 – 32Combined sources6
Helixi40 – 43Combined sources4
Turni44 – 48Combined sources5
Beta strandi52 – 56Combined sources5
Helixi62 – 72Combined sources11
Beta strandi75 – 79Combined sources5
Helixi86 – 91Combined sources6
Helixi94 – 100Combined sources7
Helixi102 – 116Combined sources15
Helixi120 – 125Combined sources6
Beta strandi127 – 133Combined sources7
Helixi134 – 137Combined sources4
Helixi143 – 145Combined sources3
Helixi166 – 185Combined sources20
Beta strandi189 – 194Combined sources6
Beta strandi196 – 199Combined sources4
Helixi207 – 217Combined sources11
Beta strandi221 – 224Combined sources4
Beta strandi230 – 235Combined sources6
Helixi236 – 249Combined sources14
Beta strandi255 – 258Combined sources4
Beta strandi263 – 265Combined sources3
Helixi266 – 280Combined sources15
Helixi287 – 290Combined sources4
Beta strandi291 – 294Combined sources4
Helixi309 – 315Combined sources7
Helixi323 – 336Combined sources14
Helixi338 – 343Combined sources6
Helixi347 – 357Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1G1AX-ray2.47A/B/C/D1-361[»]
1KEUX-ray2.40A/B1-361[»]
1KEWX-ray1.80A/B1-361[»]
ProteinModelPortaliP26391
SMRiP26391
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26391

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni206 – 207Substrate bindingCombined sources1 Publication2
Regioni222 – 224Substrate bindingCombined sources1 Publication3
Regioni296 – 300Substrate bindingCombined sources1 Publication5

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C1B Bacteria
COG1088 LUCA
HOGENOMiHOG000168006
KOiK01710
OMAiEWCQHVQ
PhylomeDBiP26391

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.

P26391-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKILITGGAG FIGSAVVRHI IKNTQDTVVN IDKLTYAGNL ESLSDISESN
60 70 80 90 100
RYNFEHADIC DSAEITRIFE QYQPDAVMHL AAESHVDRSI TGPAAFIETN
110 120 130 140 150
IVGTYALLEV ARKYWSALGE DKKNNFRFHH ISTDEVYGDL PHPDEVENSV
160 170 180 190 200
TLPLFTETTA YAPSSPYSAS KASSDHLVRA WRRTYGLPTI VTNCSNNYGP
210 220 230 240 250
YHFPEKLIPL VILNALEGKP LPIYGKGDQI RDWLYVEDHA RALHMVVTEG
260 270 280 290 300
KAGETYNIGG HNEKKNLDVV FTICDLLDEI VPKATSYREQ ITYVADRPGH
310 320 330 340 350
DRRYAIDAGK ISRELGWKPL ETFESGIRKT VEWYLANTQW VNNVKSGAYQ
360
SWIEQNYEGR Q
Length:361
Mass (Da):40,719
Last modified:August 1, 1992 - v1
Checksum:i3A574B4D917EBC57
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56793 Genomic DNA Translation: CAA40115.1
AE006468 Genomic DNA Translation: AAL21001.1
PIRiS15299
RefSeqiNP_461042.1, NC_003197.2
WP_000697840.1, NC_003197.2

Genome annotation databases

EnsemblBacteriaiAAL21001; AAL21001; STM2097
GeneIDi1253618
KEGGistm:STM2097
PATRICifig|99287.12.peg.2219

Entry informationi

Entry nameiRMLB_SALTY
AccessioniPrimary (citable) accession number: P26391
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: May 23, 2018
This is version 132 of the entry and version 1 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

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

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