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P26281 (HPPK_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase

EC=2.7.6.3
Alternative name(s):
6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase
Short name=PPPK
7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase
Short name=HPPK
Gene names
Name:folK
Ordered Locus Names:b0142, JW0138
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length159 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine = AMP + (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate.

Pathway

Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4.

Subunit structure

Monomer.

Miscellaneous

This enzyme is heat stable.

Sequence similarities

Belongs to the HPPK family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1 Ref.5
Chain2 – 1591582-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase
PRO_0000168249

Secondary structure

................................... 159
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P26281 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 67301CD634D0A174

FASTA15918,079
        10         20         30         40         50         60 
MTVAYIAIGS NLASPLEQVN AALKALGDIP ESHILTVSSF YRTPPLGPQD QPDYLNAAVA 

        70         80         90        100        110        120 
LETSLAPEEL LNHTQRIELQ QGRVRKAERW GPRTLDLDIM LFGNEVINTE RLTVPHYDMK 

       130        140        150 
NRGFMLWPLF EIAPELVFPD GEMLRQILHT RAFDKLNKW 

« Hide

References

« Hide 'large scale' references
[1]"Cloning, sequence analysis, and overexpression of Escherichia coli folK, the gene coding for 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase."
Talarico T.L., Ray P.H., Dev I.K., Merrill B.M., Dallas W.S.
J. Bacteriol. 174:5971-5977(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-20.
Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[2]"Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region."
Fujita N., Mori H., Yura T., Ishihama A.
Nucleic Acids Res. 22:1637-1639(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"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.
[5]"Purification and partial characterization of 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase and 7,8-dihydropteroate synthase from Escherichia coli MC4100."
Talarico T.L., Dev I.K., Dallas W.S., Ferone R., Ray P.H.
J. Bacteriol. 173:7029-7032(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-29.
[6]"Genetics and sequence analysis of the pcnB locus, an Escherichia coli gene involved in plasmid copy number control."
Liu J., Parkinson J.S.
J. Bacteriol. 171:1254-1261(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
[7]"Crystal structure of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, a potential target for the development of novel antimicrobial agents."
Xiao B., Shi G., Chen X., Yan H., Ji X.
Structure 7:489-496(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
[8]"2.0 A X-ray structure of the ternary complex of 7,8-dihydro-6-hydroxymethylpterinpyrophosphokinase from Escherichia coli with ATP and a substrate analogue."
Stammers D.K., Achari A., Somers D.O., Bryant P.K., Rosemond J., Scott D.L., Champness J.N.
FEBS Lett. 456:49-53(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L06495 Genomic DNA. Translation: AAB53446.1.
M20574 Genomic DNA. No translation available.
U00096 Genomic DNA. Translation: AAC73253.1.
AP009048 Genomic DNA. Translation: BAB96719.1.
PIRA43325.
RefSeqNP_414684.1. NC_000913.3.
YP_488445.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DY3X-ray2.00A2-159[»]
1EQ0NMR-A2-158[»]
1EQMX-ray1.50A2-158[»]
1EX8X-ray1.85A2-158[»]
1F9HX-ray1.50A2-158[»]
1G4CX-ray1.65A/B2-158[»]
1HKAX-ray1.50A2-159[»]
1HQ2X-ray1.25A2-158[»]
1IM6X-ray1.74A2-158[»]
1KBRX-ray1.55A2-158[»]
1Q0NX-ray1.25A2-158[»]
1RAOX-ray1.56A2-158[»]
1RB0X-ray1.35A2-158[»]
1RTZX-ray1.33A2-158[»]
1RU1X-ray1.40A/B2-158[»]
1RU2X-ray1.48A2-158[»]
1TMJX-ray1.45A2-158[»]
1TMMX-ray1.25A/B2-158[»]
2F63NMR-A2-158[»]
2F65NMR-A2-158[»]
3HCXX-ray1.75A2-159[»]
3HD1X-ray1.30A2-159[»]
3HD2X-ray1.10A2-159[»]
3HSDX-ray1.65A/B2-159[»]
3HSGX-ray1.14A2-159[»]
3HSJX-ray1.18A2-159[»]
3HSZX-ray1.40A2-159[»]
3HT0X-ray1.40A2-159[»]
3ILIX-ray1.45A2-159[»]
3ILJX-ray1.65A2-159[»]
3ILLX-ray1.73A2-159[»]
3ILOX-ray1.10A2-159[»]
3IP0X-ray0.89A2-159[»]
3KUEX-ray1.54A2-159[»]
3KUGX-ray2.00A2-159[»]
3KUHX-ray1.35A2-159[»]
3UD5X-ray2.00A2-159[»]
3UDEX-ray1.88A2-159[»]
3UDVX-ray1.88A2-159[»]
4F7VX-ray1.73A2-159[»]
ProteinModelPortalP26281.
SMRP26281. Positions 2-159.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP26281. 2 interactions.
STRING511145.b0142.

Chemistry

DrugBankDB00131. Adenosine monophosphate.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73253; AAC73253; b0142.
BAB96719; BAB96719; BAB96719.
GeneID12934036.
948792.
KEGGecj:Y75_p0139.
eco:b0142.
PATRIC32115391. VBIEscCol129921_0147.

Organism-specific databases

EchoBASEEB1348.
EcoGeneEG11374. folK.

Phylogenomic databases

eggNOGCOG0801.
HOGENOMHOG000217741.
KOK00950.
OMAYNHENIE.
OrthoDBEOG6XHC8G.
PhylomeDBP26281.
ProtClustDBPRK10239.

Enzyme and pathway databases

BioCycEcoCyc:H2PTERIDINEPYROPHOSPHOKIN-MONOMER.
ECOL316407:JW0138-MONOMER.
MetaCyc:H2PTERIDINEPYROPHOSPHOKIN-MONOMER.
SABIO-RKP26281.
UniPathwayUPA00077; UER00155.

Gene expression databases

GenevestigatorP26281.

Family and domain databases

Gene3D3.30.70.560. 1 hit.
InterProIPR000550. Hppk.
[Graphical view]
PfamPF01288. HPPK. 1 hit.
[Graphical view]
SUPFAMSSF55083. SSF55083. 1 hit.
TIGRFAMsTIGR01498. folK. 1 hit.
PROSITEPS00794. HPPK. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP26281.
PROP26281.

Entry information

Entry nameHPPK_ECOLI
AccessionPrimary (citable) accession number: P26281
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 137 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene