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Protein

Glucose-1-phosphate thymidylyltransferase 1

Gene

rfbA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis.1 Publication

Catalytic activityi

dTTP + alpha-D-glucose 1-phosphate = diphosphate + dTDP-alpha-D-glucose.1 Publication

Cofactori

Mg2+1 PublicationNote: Binds 1 Mg2+ ion per subunit.1 Publication

Kineticsi

  1. KM=20.5 µM for dTTP1 Publication
  2. KM=34 µM for glucose 1-phosphate1 Publication
  3. KM=95 µM for dTDP-glucose1 Publication
  4. KM=154 µM for PPi1 Publication
  1. Vmax=194 µmol/min/mg enzyme for the forward reaction1 Publication
  2. Vmax=360 µmol/min/mg enzyme for the reverse reaction1 Publication

pH dependencei

Optimum pH is 8.0-8.5. Active from pH 6.0 to 10.0.1 Publication

Pathwayi: dTDP-L-rhamnose biosynthesis

This protein is involved in the pathway dTDP-L-rhamnose biosynthesis, which is part of Carbohydrate biosynthesis.1 Publication
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.1 Publication
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
Metal bindingi111MagnesiumBy similarity1
Metal bindingi226MagnesiumBy similarity1

GO - Molecular functioni

  • glucose-1-phosphate thymidylyltransferase activity Source: EcoCyc
  • identical protein binding Source: EcoCyc
  • metal ion binding Source: EcoCyc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Lipopolysaccharide biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:DTDPGLUCOSEPP-MONOMER.
ECOL316407:JW2024-MONOMER.
MetaCyc:DTDPGLUCOSEPP-MONOMER.
UniPathwayiUPA00124.
UPA00281.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucose-1-phosphate thymidylyltransferase 1 (EC:2.7.7.241 Publication)
Short name:
G1P-TT 1
Alternative name(s):
dTDP-glucose pyrophosphorylase 1
dTDP-glucose synthase 1
Gene namesi
Name:rfbA
Synonyms:rmlA, rmlA1
Ordered Locus Names:b2039, JW2024
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11978. rfbA.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002079911 – 293Glucose-1-phosphate thymidylyltransferase 1Add BLAST293

Proteomic databases

EPDiP37744.
PaxDbiP37744.
PRIDEiP37744.

2D gel databases

SWISS-2DPAGEP37744.

Interactioni

Subunit structurei

Homotetramer.1 Publication

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4259680. 171 interactors.
IntActiP37744. 9 interactors.
STRINGi511145.b2039.

Structurei

Secondary structure

1293
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 9Combined sources6
Helixi15 – 17Combined sources3
Turni18 – 22Combined sources5
Helixi26 – 28Combined sources3
Beta strandi29 – 31Combined sources3
Helixi38 – 46Combined sources9
Beta strandi49 – 56Combined sources8
Turni58 – 60Combined sources3
Helixi61 – 68Combined sources8
Helixi72 – 74Combined sources3
Beta strandi77 – 82Combined sources6
Helixi91 – 95Combined sources5
Helixi97 – 100Combined sources4
Beta strandi105 – 109Combined sources5
Beta strandi113 – 115Combined sources3
Helixi119 – 128Combined sources10
Beta strandi131 – 139Combined sources9
Helixi143 – 145Combined sources3
Beta strandi146 – 151Combined sources6
Beta strandi153 – 155Combined sources3
Beta strandi157 – 163Combined sources7
Beta strandi170 – 179Combined sources10
Helixi183 – 189Combined sources7
Beta strandi194 – 197Combined sources4
Helixi200 – 209Combined sources10
Beta strandi213 – 217Combined sources5
Beta strandi222 – 225Combined sources4
Helixi230 – 247Combined sources18
Helixi254 – 260Combined sources7
Helixi266 – 273Combined sources8
Helixi274 – 276Combined sources3
Helixi280 – 288Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1H5RX-ray1.90A/B/C/D1-293[»]
1H5SX-ray2.30A/B/C/D1-293[»]
1H5TX-ray1.90A/B/C/D1-293[»]
ProteinModelPortaliP37744.
SMRiP37744.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP37744.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4108I19. Bacteria.
COG1209. LUCA.
HOGENOMiHOG000283473.
InParanoidiP37744.
KOiK00973.
OMAiPHDAEQF.
PhylomeDBiP37744.

Family and domain databases

CDDicd02538. G1P_TT_short. 1 hit.
Gene3Di3.90.550.10. 1 hit.
InterProiIPR005907. G1P_thy_trans_s.
IPR005835. NTP_transferase_dom.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR22572:SF105. PTHR22572:SF105. 1 hit.
PfamiPF00483. NTP_transferase. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
TIGRFAMsiTIGR01207. rmlA. 1 hit.

Sequencei

Sequence statusi: Complete.

P37744-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKMRKGIILA GGSGTRLYPV TMAVSKQLLP IYDKPMIYYP LSTLMLAGIR
60 70 80 90 100
DILIISTPQD TPRFQQLLGD GSQWGLNLQY KVQPSPDGLA QAFIIGEEFI
110 120 130 140 150
GGDDCALVLG DNIFYGHDLP KLMEAAVNKE SGATVFAYHV NDPERYGVVE
160 170 180 190 200
FDKNGTAISL EEKPLEPKSN YAVTGLYFYD NDVVQMAKNL KPSARGELEI
210 220 230 240 250
TDINRIYLEQ GRLSVAMMGR GYAWLDTGTH QSLIEASNFI ATIEERQGLK
260 270 280 290
VSCPEEIAFR KGFIDVEQVR KLAVPLIKNN YGQYLYKMTK DSN
Length:293
Mass (Da):32,694
Last modified:November 1, 1997 - v2
Checksum:iBA895362D1C5CA55
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti247Q → P in AAC31629 (PubMed:7517390).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09876 Genomic DNA. Translation: AAB88400.1.
U00096 Genomic DNA. Translation: AAC75100.1.
AP009048 Genomic DNA. Translation: BAA15881.1.
U03041 Genomic DNA. Translation: AAC31629.1.
PIRiF64969.
RefSeqiNP_416543.1. NC_000913.3.
WP_000783975.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75100; AAC75100; b2039.
BAA15881; BAA15881; BAA15881.
GeneIDi945154.
KEGGiecj:JW2024.
eco:b2039.
PATRICi32119411. VBIEscCol129921_2116.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09876 Genomic DNA. Translation: AAB88400.1.
U00096 Genomic DNA. Translation: AAC75100.1.
AP009048 Genomic DNA. Translation: BAA15881.1.
U03041 Genomic DNA. Translation: AAC31629.1.
PIRiF64969.
RefSeqiNP_416543.1. NC_000913.3.
WP_000783975.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1H5RX-ray1.90A/B/C/D1-293[»]
1H5SX-ray2.30A/B/C/D1-293[»]
1H5TX-ray1.90A/B/C/D1-293[»]
ProteinModelPortaliP37744.
SMRiP37744.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259680. 171 interactors.
IntActiP37744. 9 interactors.
STRINGi511145.b2039.

2D gel databases

SWISS-2DPAGEP37744.

Proteomic databases

EPDiP37744.
PaxDbiP37744.
PRIDEiP37744.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75100; AAC75100; b2039.
BAA15881; BAA15881; BAA15881.
GeneIDi945154.
KEGGiecj:JW2024.
eco:b2039.
PATRICi32119411. VBIEscCol129921_2116.

Organism-specific databases

EchoBASEiEB1921.
EcoGeneiEG11978. rfbA.

Phylogenomic databases

eggNOGiENOG4108I19. Bacteria.
COG1209. LUCA.
HOGENOMiHOG000283473.
InParanoidiP37744.
KOiK00973.
OMAiPHDAEQF.
PhylomeDBiP37744.

Enzyme and pathway databases

UniPathwayiUPA00124.
UPA00281.
BioCyciEcoCyc:DTDPGLUCOSEPP-MONOMER.
ECOL316407:JW2024-MONOMER.
MetaCyc:DTDPGLUCOSEPP-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP37744.
PROiP37744.

Family and domain databases

CDDicd02538. G1P_TT_short. 1 hit.
Gene3Di3.90.550.10. 1 hit.
InterProiIPR005907. G1P_thy_trans_s.
IPR005835. NTP_transferase_dom.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR22572:SF105. PTHR22572:SF105. 1 hit.
PfamiPF00483. NTP_transferase. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
TIGRFAMsiTIGR01207. rmlA. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRMLA1_ECOLI
AccessioniPrimary (citable) accession number: P37744
Secondary accession number(s): P78081
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: November 1, 1997
Last modified: November 2, 2016
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Both catalyzed reactions, i.e. dTDP-glucose biosynthesis and pyrophosphorolysis, follow a sequential ordered bi-bi catalytic mechanism.1 Publication

Caution

Most extant K-12 lines do not express O-antigen because of mutations in dTDP-rhamnose biosynthetic genes or in the rhamnosyltransferase gene wbbL.Curated

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.