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P26281

- HPPK_ECOLI

UniProt

P26281 - HPPK_ECOLI

Protein

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

Gene

folK

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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: EcoCyc
    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

    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.

    Pathology & Biotechi

    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 – 108
    Beta strandi12 – 143
    Helixi15 – 2713
    Beta strandi32 – 376
    Beta strandi41 – 433
    Beta strandi46 – 483
    Beta strandi49 – 513
    Beta strandi54 – 6310
    Helixi67 – 8014
    Turni82 – 865
    Beta strandi87 – 904
    Helixi91 – 933
    Beta strandi96 – 1027
    Beta strandi107 – 1115
    Beta strandi113 – 1153
    Helixi119 – 1213
    Helixi123 – 13210
    Beta strandi139 – 1413
    Helixi144 – 1518

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    KOiK00950.
    OMAiFDELSKW.
    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

    MTVAYIAIGS NLASPLEQVN AALKALGDIP ESHILTVSSF YRTPPLGPQD    50
    QPDYLNAAVA LETSLAPEEL LNHTQRIELQ QGRVRKAERW GPRTLDLDIM 100
    LFGNEVINTE RLTVPHYDMK NRGFMLWPLF EIAPELVFPD GEMLRQILHT 150
    RAFDKLNKW 159
    Length:159
    Mass (Da):18,079
    Last modified:January 23, 2007 - v3
    Checksum:i67301CD634D0A174
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi A43325.
    RefSeqi NP_414684.1. NC_000913.3.
    YP_488445.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DY3 X-ray 2.00 A 2-159 [» ]
    1EQ0 NMR - A 2-159 [» ]
    1EQM X-ray 1.50 A 2-159 [» ]
    1EX8 X-ray 1.85 A 2-159 [» ]
    1F9H X-ray 1.50 A 2-159 [» ]
    1G4C X-ray 1.65 A/B 2-159 [» ]
    1HKA X-ray 1.50 A 2-159 [» ]
    1HQ2 X-ray 1.25 A 2-159 [» ]
    1IM6 X-ray 1.74 A 2-159 [» ]
    1KBR X-ray 1.55 A 2-159 [» ]
    1Q0N X-ray 1.25 A 2-159 [» ]
    1RAO X-ray 1.56 A 2-159 [» ]
    1RB0 X-ray 1.35 A 2-159 [» ]
    1RTZ X-ray 1.33 A 2-159 [» ]
    1RU1 X-ray 1.40 A/B 2-159 [» ]
    1RU2 X-ray 1.48 A 2-159 [» ]
    1TMJ X-ray 1.45 A 2-159 [» ]
    1TMM X-ray 1.25 A/B 2-159 [» ]
    2F63 NMR - A 2-159 [» ]
    2F65 NMR - A 2-159 [» ]
    3HCX X-ray 1.75 A 2-159 [» ]
    3HD1 X-ray 1.30 A 2-159 [» ]
    3HD2 X-ray 1.10 A 2-159 [» ]
    3HSD X-ray 1.65 A/B 2-159 [» ]
    3HSG X-ray 1.14 A 2-159 [» ]
    3HSJ X-ray 1.18 A 2-159 [» ]
    3HSZ X-ray 1.40 A 2-159 [» ]
    3HT0 X-ray 1.40 A 2-159 [» ]
    3ILI X-ray 1.45 A 2-159 [» ]
    3ILJ X-ray 1.65 A 2-159 [» ]
    3ILL X-ray 1.73 A 2-159 [» ]
    3ILO X-ray 1.10 A 2-159 [» ]
    3IP0 X-ray 0.89 A 2-159 [» ]
    3KUE X-ray 1.54 A 2-159 [» ]
    3KUG X-ray 2.00 A 2-159 [» ]
    3KUH X-ray 1.35 A 2-159 [» ]
    3UD5 X-ray 2.00 A 2-159 [» ]
    3UDE X-ray 1.88 A 2-159 [» ]
    3UDV X-ray 1.88 A 2-159 [» ]
    4F7V X-ray 1.73 A 2-159 [» ]
    4M5G X-ray 1.31 A 1-159 [» ]
    4M5H X-ray 1.11 A 1-159 [» ]
    4M5I X-ray 1.08 A 1-159 [» ]
    4M5J X-ray 1.70 A 1-159 [» ]
    4M5K X-ray 1.30 A 1-159 [» ]
    4M5L X-ray 1.09 A 1-159 [» ]
    4M5M X-ray 1.12 A 1-159 [» ]
    4M5N X-ray 2.00 A/B 1-159 [» ]
    ProteinModelPortali P26281.
    SMRi P26281. Positions 2-159.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P26281. 2 interactions.
    STRINGi 511145.b0142.

    Chemistry

    DrugBanki DB00131. Adenosine monophosphate.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC73253 ; AAC73253 ; b0142 .
    BAB96719 ; BAB96719 ; BAB96719 .
    GeneIDi 12934036.
    948792.
    KEGGi ecj:Y75_p0139.
    eco:b0142.
    PATRICi 32115391. VBIEscCol129921_0147.

    Organism-specific databases

    EchoBASEi EB1348.
    EcoGenei EG11374. folK.

    Phylogenomic databases

    eggNOGi COG0801.
    HOGENOMi HOG000217741.
    KOi K00950.
    OMAi FDELSKW.
    OrthoDBi EOG6XHC8G.
    PhylomeDBi P26281.

    Enzyme and pathway databases

    UniPathwayi UPA00077 ; UER00155 .
    BioCyci EcoCyc:H2PTERIDINEPYROPHOSPHOKIN-MONOMER.
    ECOL316407:JW0138-MONOMER.
    MetaCyc:H2PTERIDINEPYROPHOSPHOKIN-MONOMER.
    SABIO-RK P26281.

    Miscellaneous databases

    EvolutionaryTracei P26281.
    PROi P26281.

    Gene expression databases

    Genevestigatori P26281.

    Family and domain databases

    Gene3Di 3.30.70.560. 1 hit.
    InterProi IPR000550. Hppk.
    [Graphical view ]
    Pfami PF01288. HPPK. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55083. SSF55083. 1 hit.
    TIGRFAMsi TIGR01498. folK. 1 hit.
    PROSITEi PS00794. HPPK. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 140 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