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 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei81 – 811NAD; via carbonyl oxygen1 Publication
Binding sitei85 – 851Substrate; via carbonyl oxygenBy similarity
Binding sitei100 – 1001NAD1 Publication
Active sitei135 – 1351Proton donor2 Publications
Active sitei136 – 1361Proton acceptor2 Publications
Active sitei160 – 1601Proton acceptor2 Publications
Binding sitei189 – 1891SubstrateBy similarity
Binding sitei190 – 1901NAD; via amide nitrogen1 Publication
Binding sitei224 – 2241SubstrateBy similarity
Binding sitei259 – 2591SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi8 – 147NAD1 Publication
Nucleotide bindingi33 – 364NAD1 Publication
Nucleotide bindingi59 – 602NAD1 Publication
Nucleotide bindingi160 – 1645NAD1 Publication

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.
RETL1328306-WGS:GSTH-1529-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11453. rffG.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 355355dTDP-glucose 4,6-dehydratase 2PRO_0000183236Add
BLAST

Proteomic databases

PaxDbiP27830.
PRIDEiP27830.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi4262077. 235 interactions.
STRINGi511145.b3788.

Structurei

Secondary structure

1
355
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 75Combined sources
Turni8 – 103Combined sources
Helixi12 – 2413Combined sources
Beta strandi28 – 325Combined sources
Helixi41 – 433Combined sources
Turni44 – 496Combined sources
Beta strandi53 – 564Combined sources
Helixi63 – 7311Combined sources
Beta strandi76 – 805Combined sources
Beta strandi91 – 933Combined sources
Helixi96 – 1016Combined sources
Helixi103 – 11715Combined sources
Helixi121 – 1266Combined sources
Beta strandi128 – 1347Combined sources
Helixi135 – 1384Combined sources
Beta strandi143 – 1453Combined sources
Helixi159 – 17820Combined sources
Beta strandi182 – 1876Combined sources
Beta strandi189 – 1924Combined sources
Helixi200 – 20910Combined sources
Beta strandi226 – 2283Combined sources
Helixi229 – 24214Combined sources
Beta strandi248 – 2514Combined sources
Helixi259 – 27315Combined sources
Helixi284 – 2874Combined sources
Helixi306 – 3116Combined sources
Helixi320 – 33314Combined sources
Helixi335 – 3439Combined sources
Helixi345 – 3484Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BXKX-ray1.90A/B1-355[»]
ProteinModelPortaliP27830.
SMRiP27830. Positions 1-350.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27830.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni134 – 1363Substrate bindingBy similarity
Regioni199 – 2002Substrate bindingBy similarity
Regioni215 – 2173Substrate bindingBy similarity
Regioni294 – 2974Substrate bindingBy similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti314 – 3152WL → CV in AAA67588 (PubMed:1379743).Curated

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1BXKX-ray1.90A/B1-355[»]
ProteinModelPortaliP27830.
SMRiP27830. Positions 1-350.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262077. 235 interactions.
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.
RETL1328306-WGS:GSTH-1529-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: September 7, 2016
This is version 138 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.