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Protein

2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase

Gene

folK

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Pathwayi

GO - Molecular functioni

  1. 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity Source: EcoliWiki
  2. ATP binding Source: UniProtKB-KW
  3. kinase activity Source: UniProtKB-KW
  4. magnesium ion binding Source: EcoCyc

GO - Biological processi

  1. folic acid biosynthetic process Source: UniProtKB-KW
  2. tetrahydrofolate biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Folate biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:H2PTERIDINEPYROPHOSPHOKIN-MONOMER.
ECOL316407:JW0138-MONOMER.
MetaCyc:H2PTERIDINEPYROPHOSPHOKIN-MONOMER.
SABIO-RKP26281.
UniPathwayiUPA00077; UER00155.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:folK
Ordered Locus Names:b0142, JW0138
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG11374. folK.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 1591582-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinasePRO_0000168249Add
BLAST

Expressioni

Gene expression databases

GenevestigatoriP26281.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

IntActiP26281. 2 interactions.
STRINGi511145.b0142.

Structurei

Secondary structure

1
159
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 108Combined sources
Beta strandi12 – 143Combined sources
Helixi15 – 2713Combined sources
Beta strandi32 – 376Combined sources
Beta strandi41 – 433Combined sources
Beta strandi46 – 483Combined sources
Beta strandi49 – 513Combined sources
Beta strandi54 – 6310Combined sources
Helixi67 – 8014Combined sources
Turni82 – 865Combined sources
Beta strandi87 – 904Combined sources
Helixi91 – 933Combined sources
Beta strandi96 – 1027Combined sources
Beta strandi107 – 1115Combined sources
Beta strandi113 – 1153Combined sources
Helixi119 – 1213Combined sources
Helixi123 – 13210Combined sources
Beta strandi139 – 1413Combined sources
Helixi144 – 1518Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DY3X-ray2.00A2-159[»]
1EQ0NMR-A2-159[»]
1EQMX-ray1.50A2-159[»]
1EX8X-ray1.85A2-159[»]
1F9HX-ray1.50A2-159[»]
1G4CX-ray1.65A/B2-159[»]
1HKAX-ray1.50A2-159[»]
1HQ2X-ray1.25A2-159[»]
1IM6X-ray1.74A2-159[»]
1KBRX-ray1.55A2-159[»]
1Q0NX-ray1.25A2-159[»]
1RAOX-ray1.56A2-159[»]
1RB0X-ray1.35A2-159[»]
1RTZX-ray1.33A2-159[»]
1RU1X-ray1.40A/B2-159[»]
1RU2X-ray1.48A2-159[»]
1TMJX-ray1.45A2-159[»]
1TMMX-ray1.25A/B2-159[»]
2F63NMR-A2-159[»]
2F65NMR-A2-159[»]
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[»]
4M5GX-ray1.31A1-159[»]
4M5HX-ray1.11A1-159[»]
4M5IX-ray1.08A1-159[»]
4M5JX-ray1.70A1-159[»]
4M5KX-ray1.30A1-159[»]
4M5LX-ray1.09A1-159[»]
4M5MX-ray1.12A1-159[»]
4M5NX-ray2.00A/B1-159[»]
ProteinModelPortaliP26281.
SMRiP26281. Positions 2-159.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26281.

Family & Domainsi

Sequence similaritiesi

Belongs to the HPPK family.Curated

Phylogenomic databases

eggNOGiCOG0801.
HOGENOMiHOG000217741.
InParanoidiP26281.
KOiK00950.
OMAiDVLAYEG.
OrthoDBiEOG6XHC8G.
PhylomeDBiP26281.

Family and domain databases

Gene3Di3.30.70.560. 1 hit.
InterProiIPR000550. Hppk.
[Graphical view]
PfamiPF01288. HPPK. 1 hit.
[Graphical view]
SUPFAMiSSF55083. SSF55083. 1 hit.
TIGRFAMsiTIGR01498. folK. 1 hit.
PROSITEiPS00794. HPPK. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P26281-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTVAYIAIGS NLASPLEQVN AALKALGDIP ESHILTVSSF YRTPPLGPQD
60 70 80 90 100
QPDYLNAAVA LETSLAPEEL LNHTQRIELQ QGRVRKAERW GPRTLDLDIM
110 120 130 140 150
LFGNEVINTE RLTVPHYDMK NRGFMLWPLF EIAPELVFPD GEMLRQILHT

RAFDKLNKW
Length:159
Mass (Da):18,079
Last modified:January 23, 2007 - v3
Checksum:i67301CD634D0A174
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06495 Genomic DNA. Translation: AAB53446.1.
M20574 Genomic DNA. No translation available.
U00096 Genomic DNA. Translation: AAC73253.1.
AP009048 Genomic DNA. Translation: BAB96719.1.
PIRiA43325.
RefSeqiNP_414684.1. NC_000913.3.
YP_488445.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73253; AAC73253; b0142.
BAB96719; BAB96719; BAB96719.
GeneIDi12934036.
948792.
KEGGiecj:Y75_p0139.
eco:b0142.
PATRICi32115391. VBIEscCol129921_0147.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06495 Genomic DNA. Translation: AAB53446.1.
M20574 Genomic DNA. No translation available.
U00096 Genomic DNA. Translation: AAC73253.1.
AP009048 Genomic DNA. Translation: BAB96719.1.
PIRiA43325.
RefSeqiNP_414684.1. NC_000913.3.
YP_488445.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DY3X-ray2.00A2-159[»]
1EQ0NMR-A2-159[»]
1EQMX-ray1.50A2-159[»]
1EX8X-ray1.85A2-159[»]
1F9HX-ray1.50A2-159[»]
1G4CX-ray1.65A/B2-159[»]
1HKAX-ray1.50A2-159[»]
1HQ2X-ray1.25A2-159[»]
1IM6X-ray1.74A2-159[»]
1KBRX-ray1.55A2-159[»]
1Q0NX-ray1.25A2-159[»]
1RAOX-ray1.56A2-159[»]
1RB0X-ray1.35A2-159[»]
1RTZX-ray1.33A2-159[»]
1RU1X-ray1.40A/B2-159[»]
1RU2X-ray1.48A2-159[»]
1TMJX-ray1.45A2-159[»]
1TMMX-ray1.25A/B2-159[»]
2F63NMR-A2-159[»]
2F65NMR-A2-159[»]
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[»]
4M5GX-ray1.31A1-159[»]
4M5HX-ray1.11A1-159[»]
4M5IX-ray1.08A1-159[»]
4M5JX-ray1.70A1-159[»]
4M5KX-ray1.30A1-159[»]
4M5LX-ray1.09A1-159[»]
4M5MX-ray1.12A1-159[»]
4M5NX-ray2.00A/B1-159[»]
ProteinModelPortaliP26281.
SMRiP26281. Positions 2-159.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP26281. 2 interactions.
STRINGi511145.b0142.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73253; AAC73253; b0142.
BAB96719; BAB96719; BAB96719.
GeneIDi12934036.
948792.
KEGGiecj:Y75_p0139.
eco:b0142.
PATRICi32115391. VBIEscCol129921_0147.

Organism-specific databases

EchoBASEiEB1348.
EcoGeneiEG11374. folK.

Phylogenomic databases

eggNOGiCOG0801.
HOGENOMiHOG000217741.
InParanoidiP26281.
KOiK00950.
OMAiDVLAYEG.
OrthoDBiEOG6XHC8G.
PhylomeDBiP26281.

Enzyme and pathway databases

UniPathwayiUPA00077; UER00155.
BioCyciEcoCyc:H2PTERIDINEPYROPHOSPHOKIN-MONOMER.
ECOL316407:JW0138-MONOMER.
MetaCyc:H2PTERIDINEPYROPHOSPHOKIN-MONOMER.
SABIO-RKP26281.

Miscellaneous databases

EvolutionaryTraceiP26281.
PROiP26281.

Gene expression databases

GenevestigatoriP26281.

Family and domain databases

Gene3Di3.30.70.560. 1 hit.
InterProiIPR000550. Hppk.
[Graphical view]
PfamiPF01288. HPPK. 1 hit.
[Graphical view]
SUPFAMiSSF55083. SSF55083. 1 hit.
TIGRFAMsiTIGR01498. folK. 1 hit.
PROSITEiPS00794. HPPK. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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).

Entry informationi

Entry nameiHPPK_ECOLI
AccessioniPrimary (citable) accession number: P26281
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 23, 2007
Last modified: January 7, 2015
This is version 143 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

This enzyme is heat stable.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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

External Data

Dasty 3

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 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.