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Protein

dTDP-glucose 4,6-dehydratase 2

Gene

rffG

Organism
Escherichia coli (strain K12)
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.3 Publications

Catalytic activityi

dTDP-alpha-D-glucose = dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O.3 Publications

Cofactori

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

Pathwayi: dTDP-4-acetamido-4,6-dideoxygalactose biosynthesis

This protein is involved in the pathway dTDP-4-acetamido-4,6-dideoxygalactose biosynthesis, which is part of Nucleotide-sugar biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway dTDP-4-acetamido-4,6-dideoxygalactose biosynthesis and in Nucleotide-sugar biosynthesis.

Pathwayi: enterobacterial common antigen biosynthesis

This protein is involved in the pathway enterobacterial common antigen biosynthesis, which is part of Bacterial outer membrane biogenesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway enterobacterial common antigen biosynthesis and in Bacterial outer membrane biogenesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei81NAD; via carbonyl oxygen1 Publication1
Binding sitei85Substrate; via carbonyl oxygenBy similarity1
Binding sitei100NAD1 Publication1
Active sitei135Proton donor2 Publications1
Active sitei136Proton acceptor2 Publications1
Active sitei160Proton acceptor2 Publications1
Binding sitei189SubstrateBy similarity1
Binding sitei190NAD; via amide nitrogen1 Publication1
Binding sitei224SubstrateBy similarity1
Binding sitei259SubstrateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi8 – 14NAD1 Publication7
Nucleotide bindingi33 – 36NAD1 Publication4
Nucleotide bindingi59 – 60NAD1 Publication2
Nucleotide bindingi160 – 164NAD1 Publication5

GO - Molecular functioni

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciEcoCyc:DTDPGLUCDEHYDRAT2-MONOMER.
ECOL316407:JW5598-MONOMER.
MetaCyc:DTDPGLUCDEHYDRAT2-MONOMER.
BRENDAi4.2.1.46. 2026.
SABIO-RKP27830.
UniPathwayiUPA00566.
UPA00817.

Names & Taxonomyi

Protein namesi
Recommended name:
dTDP-glucose 4,6-dehydratase 2 (EC:4.2.1.463 Publications)
Gene namesi
Name:rffG
Ordered Locus Names:b3788, JW5598
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11453. rffG.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001832361 – 355dTDP-glucose 4,6-dehydratase 2Add BLAST355

Proteomic databases

PaxDbiP27830.
PRIDEiP27830.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi4262077. 235 interactors.
STRINGi511145.b3788.

Structurei

Secondary structure

1355
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 7Combined sources5
Turni8 – 10Combined sources3
Helixi12 – 24Combined sources13
Beta strandi28 – 32Combined sources5
Helixi41 – 43Combined sources3
Turni44 – 49Combined sources6
Beta strandi53 – 56Combined sources4
Helixi63 – 73Combined sources11
Beta strandi76 – 80Combined sources5
Beta strandi91 – 93Combined sources3
Helixi96 – 101Combined sources6
Helixi103 – 117Combined sources15
Helixi121 – 126Combined sources6
Beta strandi128 – 134Combined sources7
Helixi135 – 138Combined sources4
Beta strandi143 – 145Combined sources3
Helixi159 – 178Combined sources20
Beta strandi182 – 187Combined sources6
Beta strandi189 – 192Combined sources4
Helixi200 – 209Combined sources10
Beta strandi226 – 228Combined sources3
Helixi229 – 242Combined sources14
Beta strandi248 – 251Combined sources4
Helixi259 – 273Combined sources15
Helixi284 – 287Combined sources4
Helixi306 – 311Combined sources6
Helixi320 – 333Combined sources14
Helixi335 – 343Combined sources9
Helixi345 – 348Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BXKX-ray1.90A/B1-355[»]
ProteinModelPortaliP27830.
SMRiP27830.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27830.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni134 – 136Substrate bindingBy similarity3
Regioni199 – 200Substrate bindingBy similarity2
Regioni215 – 217Substrate bindingBy similarity3
Regioni294 – 297Substrate bindingBy similarity4

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C1B. Bacteria.
COG1088. LUCA.
HOGENOMiHOG000168006.
InParanoidiP27830.
KOiK01710.
OMAiREWIDRQ.
PhylomeDBiP27830.

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.

P27830-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRKILITGGA GFIGSALVRY IINETSDAVV VVDKLTYAGN LMSLAPVAQS
60 70 80 90 100
ERFAFEKVDI CDRAELARVF TEHQPDCVMH LAAESHVDRS IDGPAAFIET
110 120 130 140 150
NIVGTYTLLE AARAYWNALT EDKKSAFRFH HISTDEVYGD LHSTDDFFTE
160 170 180 190 200
TTPYAPSSPY SASKASSDHL VRAWLRTYGL PTLITNCSNN YGPYHFPEKL
210 220 230 240 250
IPLMILNALA GKSLPVYGNG QQIRDWLYVE DHARALYCVA TTGKVGETYN
260 270 280 290 300
IGGHNERKNL DVVETICELL EELAPNKPHG VAHYRDLITF VADRPGHDLR
310 320 330 340 350
YAIDASKIAR ELGWLPQETF ESGMRKTVQW YLANESWWKQ VQDGSYQGER

LGLKG
Length:355
Mass (Da):39,754
Last modified:November 23, 2004 - v3
Checksum:i34DBD1EFB42DB9B3
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti314 – 315WL → CV in AAA67588 (PubMed:1379743).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M87049 Genomic DNA. Translation: AAA67588.1.
U00096 Genomic DNA. Translation: AAT48213.1.
AP009048 Genomic DNA. Translation: BAE77510.1.
PIRiG65182.
RefSeqiWP_001226601.1. NZ_LN832404.1.
YP_026255.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAT48213; AAT48213; b3788.
BAE77510; BAE77510; BAE77510.
GeneIDi948300.
KEGGiecj:JW5598.
eco:b3788.
PATRICi32123069. VBIEscCol129921_3904.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M87049 Genomic DNA. Translation: AAA67588.1.
U00096 Genomic DNA. Translation: AAT48213.1.
AP009048 Genomic DNA. Translation: BAE77510.1.
PIRiG65182.
RefSeqiWP_001226601.1. NZ_LN832404.1.
YP_026255.1. NC_000913.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BXKX-ray1.90A/B1-355[»]
ProteinModelPortaliP27830.
SMRiP27830.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262077. 235 interactors.
STRINGi511145.b3788.

Proteomic databases

PaxDbiP27830.
PRIDEiP27830.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAT48213; AAT48213; b3788.
BAE77510; BAE77510; BAE77510.
GeneIDi948300.
KEGGiecj:JW5598.
eco:b3788.
PATRICi32123069. VBIEscCol129921_3904.

Organism-specific databases

EchoBASEiEB1422.
EcoGeneiEG11453. rffG.

Phylogenomic databases

eggNOGiENOG4105C1B. Bacteria.
COG1088. LUCA.
HOGENOMiHOG000168006.
InParanoidiP27830.
KOiK01710.
OMAiREWIDRQ.
PhylomeDBiP27830.

Enzyme and pathway databases

UniPathwayiUPA00566.
UPA00817.
BioCyciEcoCyc:DTDPGLUCDEHYDRAT2-MONOMER.
ECOL316407:JW5598-MONOMER.
MetaCyc:DTDPGLUCDEHYDRAT2-MONOMER.
BRENDAi4.2.1.46. 2026.
SABIO-RKP27830.

Miscellaneous databases

EvolutionaryTraceiP27830.
PROiP27830.

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 nameiRMLB2_ECOLI
AccessioniPrimary (citable) accession number: P27830
Secondary accession number(s): P76754, Q2M896, Q6BF01
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: November 23, 2004
Last modified: November 2, 2016
This is version 139 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Was originally thought to be rffE, the UDP-N-acetylglucosamine epimerase.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.