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Protein

Glucose-1-phosphate thymidylyltransferase 2

Gene

rffH

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

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
Metal bindingi108Magnesium1 Publication1
Metal bindingi223Magnesium1 Publication1

GO - Molecular functioni

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Exopolysaccharide synthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:DTDPGLUCOSEPP2-MONOMER.
ECOL316407:JW3763-MONOMER.
MetaCyc:DTDPGLUCOSEPP2-MONOMER.
UniPathwayiUPA00566.
UPA00817.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucose-1-phosphate thymidylyltransferase 2 (EC:2.7.7.241 Publication)
Short name:
G1P-TT 2
Alternative name(s):
dTDP-glucose pyrophosphorylase 2
dTDP-glucose synthase 2
Gene namesi
Name:rffH
Synonyms:rmlA2, yifG
Ordered Locus Names:b3789, JW3763
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11454. rffH.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002079921 – 293Glucose-1-phosphate thymidylyltransferase 2Add BLAST293

Proteomic databases

PaxDbiP61887.
PRIDEiP61887.

Interactioni

Subunit structurei

Homotetramer; arranged as a dimer of dimers.1 Publication

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4261364. 234 interactors.
DIPiDIP-10689N.
IntActiP61887. 5 interactors.
STRINGi511145.b3789.

Structurei

Secondary structure

1293
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 6Combined sources5
Helixi12 – 14Combined sources3
Helixi15 – 18Combined sources4
Helixi23 – 25Combined sources3
Beta strandi26 – 28Combined sources3
Helixi35 – 43Combined sources9
Beta strandi48 – 53Combined sources6
Turni55 – 57Combined sources3
Helixi58 – 65Combined sources8
Helixi69 – 71Combined sources3
Beta strandi74 – 79Combined sources6
Helixi88 – 92Combined sources5
Helixi94 – 97Combined sources4
Beta strandi102 – 106Combined sources5
Beta strandi109 – 112Combined sources4
Helixi117 – 123Combined sources7
Beta strandi128 – 136Combined sources9
Beta strandi141 – 145Combined sources5
Beta strandi147 – 149Combined sources3
Beta strandi152 – 156Combined sources5
Beta strandi167 – 175Combined sources9
Helixi179 – 185Combined sources7
Beta strandi191 – 194Combined sources4
Helixi197 – 206Combined sources10
Beta strandi210 – 214Combined sources5
Beta strandi220 – 223Combined sources4
Helixi227 – 244Combined sources18
Helixi251 – 257Combined sources7
Helixi263 – 272Combined sources10
Turni273 – 275Combined sources3
Helixi277 – 284Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MC3X-ray2.60A/B1-293[»]
ProteinModelPortaliP61887.
SMRiP61887.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP61887.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4108I19. Bacteria.
COG1209. LUCA.
HOGENOMiHOG000283473.
InParanoidiP61887.
KOiK00973.
OMAiIMLSGIR.
PhylomeDBiP61887.

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.

P61887-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKGIILAGGS GTRLHPITRG VSKQLLPIYD KPMIYYPLSV LMLAGIREIL
60 70 80 90 100
IITTPEDKGY FQRLLGDGSE FGIQLEYAEQ PSPDGLAQAF IIGETFLNGE
110 120 130 140 150
PSCLVLGDNI FFGQGFSPKL RHVAARTEGA TVFGYQVMDP ERFGVVEFDD
160 170 180 190 200
NFRAISLEEK PKQPKSNWAV TGLYFYDSKV VEYAKQVKPS ERGELEITSI
210 220 230 240 250
NQMYLEAGNL TVELLGRGFA WLDTGTHDSL IEASTFVQTV EKRQGFKIAC
260 270 280 290
LEEIAWRNGW LDDEGVKRAA SSLAKTGYGQ YLLELLRARP RQY
Length:293
Mass (Da):32,734
Last modified:June 7, 2004 - v1
Checksum:i5DA66676CD8F9139
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti5I → M in AAA67589 (PubMed:1379743).Curated1
Sequence conflicti68 – 69GS → VG in AAA67589 (PubMed:1379743).Curated2
Sequence conflicti130 – 131AT → P in AAA67589 (PubMed:1379743).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M87049 Genomic DNA. Translation: AAA67589.1.
U00096 Genomic DNA. Translation: AAC76794.1.
AP009048 Genomic DNA. Translation: BAE77509.1.
PIRiH65182.
RefSeqiNP_418236.1. NC_000913.3.
WP_000676056.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76794; AAC76794; b3789.
BAE77509; BAE77509; BAE77509.
GeneIDi948299.
KEGGiecj:JW3763.
eco:b3789.
PATRICi32123071. VBIEscCol129921_3905.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M87049 Genomic DNA. Translation: AAA67589.1.
U00096 Genomic DNA. Translation: AAC76794.1.
AP009048 Genomic DNA. Translation: BAE77509.1.
PIRiH65182.
RefSeqiNP_418236.1. NC_000913.3.
WP_000676056.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MC3X-ray2.60A/B1-293[»]
ProteinModelPortaliP61887.
SMRiP61887.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261364. 234 interactors.
DIPiDIP-10689N.
IntActiP61887. 5 interactors.
STRINGi511145.b3789.

Proteomic databases

PaxDbiP61887.
PRIDEiP61887.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76794; AAC76794; b3789.
BAE77509; BAE77509; BAE77509.
GeneIDi948299.
KEGGiecj:JW3763.
eco:b3789.
PATRICi32123071. VBIEscCol129921_3905.

Organism-specific databases

EchoBASEiEB1423.
EcoGeneiEG11454. rffH.

Phylogenomic databases

eggNOGiENOG4108I19. Bacteria.
COG1209. LUCA.
HOGENOMiHOG000283473.
InParanoidiP61887.
KOiK00973.
OMAiIMLSGIR.
PhylomeDBiP61887.

Enzyme and pathway databases

UniPathwayiUPA00566.
UPA00817.
BioCyciEcoCyc:DTDPGLUCOSEPP2-MONOMER.
ECOL316407:JW3763-MONOMER.
MetaCyc:DTDPGLUCOSEPP2-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP61887.
PROiP61887.

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 nameiRMLA2_ECOLI
AccessioniPrimary (citable) accession number: P61887
Secondary accession number(s): P27831, P76755, Q2M897
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: November 2, 2016
This is version 115 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. 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.