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

rfbB

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed-Annotation score: Annotation score: 5 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.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.
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.
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 sitei80NAD; via carbonyl oxygen2 Publications1
Binding sitei84Substrate; via carbonyl oxygen1 Publication1
Binding sitei99NAD2 Publications1
Active sitei134Proton donor1 Publication1
Active sitei135Proton acceptor1 Publication1
Active sitei167Proton acceptor1 Publication1
Binding sitei196Substrate1 Publication1
Binding sitei197NAD; via amide nitrogen2 Publications1
Binding sitei231Substrate1 Publication1
Binding sitei266Substrate1 Publication1
Binding sitei357Substrate1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi10 – 12NAD2 Publications3
Nucleotide bindingi32 – 35NAD2 Publications4
Nucleotide bindingi58 – 59NAD2 Publications2
Nucleotide bindingi167 – 171NAD2 Publications5

GO - Molecular functioni

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Lipopolysaccharide biosynthesis

Keywords - Ligandi

NAD

Enzyme and pathway databases

SABIO-RKP26391.
UniPathwayiUPA00124.
UPA00281.

Names & Taxonomyi

Protein namesi
Recommended name:
dTDP-glucose 4,6-dehydratase (EC:4.2.1.46)
Gene namesi
Name:rfbB
Ordered Locus Names:STM2097
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeSalmonella
Proteomesi
  • UP000001014 Componenti: Chromosome

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
Regioni133 – 135Substrate binding3
Regioni206 – 207Substrate binding2
Regioni222 – 224Substrate binding3
Regioni297 – 300Substrate binding4

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C1B. Bacteria.
COG1088. LUCA.
HOGENOMiHOG000168006.
KOiK01710.
OMAiARHYWMQ.
PhylomeDBiP26391.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR005888. dTDP_Gluc_deHydtase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR10366:SF41. PTHR10366:SF41. 1 hit.
PfamiPF16363. GDP_Man_Dehyd. 1 hit.
[Graphical view]
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_003197.1.
WP_000697840.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL21001; AAL21001; STM2097.
GeneIDi1253618.
KEGGistm:STM2097.
PATRICi32382777. VBISalEnt20916_2219.

Cross-referencesi

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_003197.1.
WP_000697840.1. NC_003197.1.

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...

Protein-protein interaction databases

STRINGi99287.STM2097.

Proteomic databases

PaxDbiP26391.
PRIDEiP26391.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL21001; AAL21001; STM2097.
GeneIDi1253618.
KEGGistm:STM2097.
PATRICi32382777. VBISalEnt20916_2219.

Phylogenomic databases

eggNOGiENOG4105C1B. Bacteria.
COG1088. LUCA.
HOGENOMiHOG000168006.
KOiK01710.
OMAiARHYWMQ.
PhylomeDBiP26391.

Enzyme and pathway databases

UniPathwayiUPA00124.
UPA00281.
SABIO-RKP26391.

Miscellaneous databases

EvolutionaryTraceiP26391.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR005888. dTDP_Gluc_deHydtase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR10366:SF41. PTHR10366:SF41. 1 hit.
PfamiPF16363. GDP_Man_Dehyd. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01181. dTDP_gluc_dehyt. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRMLB_SALTY
AccessioniPrimary (citable) accession number: P26391
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: November 2, 2016
This is version 124 of the entry and version 1 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.