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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi108 – 1081Magnesium1 Publication
Metal bindingi223 – 2231Magnesium1 Publication

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 293293Glucose-1-phosphate thymidylyltransferase 2PRO_0000207992Add
BLAST

Proteomic databases

EPDiP61887.
PaxDbiP61887.

Interactioni

Subunit structurei

Homotetramer; arranged as a dimer of dimers.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
groLP0A6F51EBI-550893,EBI-543750

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

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

Structurei

Secondary structure

1
293
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65Combined sources
Helixi12 – 143Combined sources
Helixi15 – 184Combined sources
Helixi23 – 253Combined sources
Beta strandi26 – 283Combined sources
Helixi35 – 439Combined sources
Beta strandi48 – 536Combined sources
Turni55 – 573Combined sources
Helixi58 – 658Combined sources
Helixi69 – 713Combined sources
Beta strandi74 – 796Combined sources
Helixi88 – 925Combined sources
Helixi94 – 974Combined sources
Beta strandi102 – 1065Combined sources
Beta strandi109 – 1124Combined sources
Helixi117 – 1237Combined sources
Beta strandi128 – 1369Combined sources
Beta strandi141 – 1455Combined sources
Beta strandi147 – 1493Combined sources
Beta strandi152 – 1565Combined sources
Beta strandi167 – 1759Combined sources
Helixi179 – 1857Combined sources
Beta strandi191 – 1944Combined sources
Helixi197 – 20610Combined sources
Beta strandi210 – 2145Combined sources
Beta strandi220 – 2234Combined sources
Helixi227 – 24418Combined sources
Helixi251 – 2577Combined sources
Helixi263 – 27210Combined sources
Turni273 – 2753Combined sources
Helixi277 – 2848Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MC3X-ray2.60A/B1-293[»]
ProteinModelPortaliP61887.
SMRiP61887. Positions 1-290.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP61887.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4108I19. Bacteria.
COG1209. LUCA.
HOGENOMiHOG000283473.
InParanoidiP61887.
KOiK00973.
OMAiPMAKNEY.
OrthoDBiEOG6RC3RN.
PhylomeDBiP61887.

Family and domain databases

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51I → M in AAA67589 (PubMed:1379743).Curated
Sequence conflicti68 – 692GS → VG in AAA67589 (PubMed:1379743).Curated
Sequence conflicti130 – 1312AT → P in AAA67589 (PubMed:1379743).Curated

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1MC3X-ray2.60A/B1-293[»]
ProteinModelPortaliP61887.
SMRiP61887. Positions 1-290.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Proteomic databases

EPDiP61887.
PaxDbiP61887.

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.
OMAiPMAKNEY.
OrthoDBiEOG6RC3RN.
PhylomeDBiP61887.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP61887.
PROiP61887.

Family and domain databases

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...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes."
    Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.
    Science 257:771-778(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Genetic analysis of the dTDP-rhamnose biosynthesis region of the Escherichia coli VW187 (O7:K1) rfb gene cluster: identification of functional homologs of rfbB and rfbA in the rff cluster and correct location of the rffE gene."
    Marolda C.L., Valvano M.A.
    J. Bacteriol. 177:5539-5546(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY.
    Strain: K12.
  5. "Crystal structure of Escherichia coli glucose-1-phosphate thymidylyltransferase (RffH) complexed with dTTP and Mg2+."
    Sivaraman J., Sauve V., Matte A., Cygler M.
    J. Biol. Chem. 277:44214-44219(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF COMPLEX WITH DTTP, COFACTOR, SUBUNIT.

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: March 16, 2016
This is version 111 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.