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P27213

- PTPS_RAT

UniProt

P27213 - PTPS_RAT

Protein

6-pyruvoyl tetrahydrobiopterin synthase

Gene

Pts

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Involved in the biosynthesis of tetrahydrobiopterin, an essential cofactor of aromatic amino acid hydroxylases. Catalyzes the transformation of 7,8-dihydroneopterin triphosphate into 6-pyruvoyl tetrahydropterin.

    Catalytic activityi

    7,8-dihydroneopterin 3'-triphosphate = 6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate.

    Cofactori

    Binds 1 zinc ion per subunit.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi23 – 231Zinc
    Active sitei42 – 421Proton acceptor
    Metal bindingi48 – 481Zinc
    Metal bindingi50 – 501Zinc
    Active sitei89 – 891Charge relay system
    Active sitei133 – 1331Charge relay system

    GO - Molecular functioni

    1. 6-pyruvoyltetrahydropterin synthase activity Source: RGD
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. tetrahydrobiopterin biosynthetic process Source: RGD

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Tetrahydrobiopterin biosynthesis

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BRENDAi4.2.3.12. 5301.
    ReactomeiREACT_199128. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
    UniPathwayiUPA00849; UER00819.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    6-pyruvoyl tetrahydrobiopterin synthase (EC:4.2.3.12)
    Short name:
    PTP synthase
    Short name:
    PTPS
    Gene namesi
    Name:Pts
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 8

    Organism-specific databases

    RGDi68367. Pts.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrion Source: Ensembl

    Pathology & Biotechi

    Involvement in diseasei

    Deficiency leads to phenylketonuria.

    Keywords - Diseasei

    Phenylketonuria

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 44PRO_0000029868
    Chaini5 – 1441406-pyruvoyl tetrahydrobiopterin synthasePRO_0000029869Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei18 – 181PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylation of Ser-18 is required for maximal enzyme activity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP27213.
    PRIDEiP27213.

    PTM databases

    PhosphoSiteiP27213.

    Expressioni

    Gene expression databases

    GenevestigatoriP27213.

    Interactioni

    Subunit structurei

    Homohexamer formed of two homotrimers in a head to head fashion.

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000012434.

    Structurei

    Secondary structure

    1
    144
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi10 – 2314
    Helixi32 – 398
    Helixi40 – 434
    Beta strandi48 – 6114
    Turni64 – 663
    Helixi72 – 8211
    Helixi84 – 874
    Helixi92 – 954
    Helixi97 – 993
    Beta strandi100 – 1023
    Helixi106 – 12015
    Turni123 – 1253
    Beta strandi126 – 1349
    Beta strandi137 – 1415

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1B66X-ray1.90A/B5-144[»]
    1B6ZX-ray2.00A/B5-144[»]
    1GTQX-ray2.30A/B5-144[»]
    ProteinModelPortaliP27213.
    SMRiP27213. Positions 8-144.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP27213.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PTPS family.Curated

    Phylogenomic databases

    eggNOGiCOG0720.
    GeneTreeiENSGT00390000002752.
    HOGENOMiHOG000225069.
    HOVERGENiHBG004358.
    InParanoidiP27213.
    KOiK01737.
    OMAiCHRLHSK.
    OrthoDBiEOG7NSB3V.
    PhylomeDBiP27213.
    TreeFamiTF105796.

    Family and domain databases

    InterProiIPR007115. 6-PTP_synth/QueD.
    IPR022470. PTPS_Cys_AS.
    IPR022469. PTPS_His_AS.
    [Graphical view]
    PANTHERiPTHR12589. PTHR12589. 1 hit.
    PfamiPF01242. PTPS. 1 hit.
    [Graphical view]
    PIRSFiPIRSF006113. PTP_synth. 1 hit.
    TIGRFAMsiTIGR00039. 6PTHBS. 1 hit.
    PROSITEiPS00987. PTPS_1. 1 hit.
    PS00988. PTPS_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P27213-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNAAVGLRRR ARLSRLVSFS ASHRLHSPSL SAEENLKVFG KCNNPNGHGH    50
    NYKVVVTIHG EIDPVTGMVM NLTDLKEYME EAIMKPLDHK NLDLDVPYFA 100
    DVVSTTENVA VYIWENLQRL LPVGALYKVK VYETDNNIVV YKGE 144
    Length:144
    Mass (Da):16,241
    Last modified:August 1, 1992 - v1
    Checksum:i0657C78F87C6FC3B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M77850 mRNA. Translation: AAA40625.1.
    BC059140 mRNA. Translation: AAH59140.1.
    PIRiA39499.
    RefSeqiNP_058916.1. NM_017220.1.
    UniGeneiRn.87164.

    Genome annotation databases

    EnsembliENSRNOT00000012434; ENSRNOP00000012434; ENSRNOG00000009250.
    GeneIDi29498.
    KEGGirno:29498.
    UCSCiRGD:68367. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M77850 mRNA. Translation: AAA40625.1 .
    BC059140 mRNA. Translation: AAH59140.1 .
    PIRi A39499.
    RefSeqi NP_058916.1. NM_017220.1.
    UniGenei Rn.87164.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1B66 X-ray 1.90 A/B 5-144 [» ]
    1B6Z X-ray 2.00 A/B 5-144 [» ]
    1GTQ X-ray 2.30 A/B 5-144 [» ]
    ProteinModelPortali P27213.
    SMRi P27213. Positions 8-144.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000012434.

    PTM databases

    PhosphoSitei P27213.

    Proteomic databases

    PaxDbi P27213.
    PRIDEi P27213.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000012434 ; ENSRNOP00000012434 ; ENSRNOG00000009250 .
    GeneIDi 29498.
    KEGGi rno:29498.
    UCSCi RGD:68367. rat.

    Organism-specific databases

    CTDi 5805.
    RGDi 68367. Pts.

    Phylogenomic databases

    eggNOGi COG0720.
    GeneTreei ENSGT00390000002752.
    HOGENOMi HOG000225069.
    HOVERGENi HBG004358.
    InParanoidi P27213.
    KOi K01737.
    OMAi CHRLHSK.
    OrthoDBi EOG7NSB3V.
    PhylomeDBi P27213.
    TreeFami TF105796.

    Enzyme and pathway databases

    UniPathwayi UPA00849 ; UER00819 .
    BRENDAi 4.2.3.12. 5301.
    Reactomei REACT_199128. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.

    Miscellaneous databases

    EvolutionaryTracei P27213.
    NextBioi 609392.
    PROi P27213.

    Gene expression databases

    Genevestigatori P27213.

    Family and domain databases

    InterProi IPR007115. 6-PTP_synth/QueD.
    IPR022470. PTPS_Cys_AS.
    IPR022469. PTPS_His_AS.
    [Graphical view ]
    PANTHERi PTHR12589. PTHR12589. 1 hit.
    Pfami PF01242. PTPS. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF006113. PTP_synth. 1 hit.
    TIGRFAMsi TIGR00039. 6PTHBS. 1 hit.
    PROSITEi PS00987. PTPS_1. 1 hit.
    PS00988. PTPS_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Purification and cDNA cloning of rat 6-pyruvoyl-tetrahydropterin synthase."
      Inoue Y., Kawasaki Y., Harada T., Hatakeyama K., Kagamiyama H.
      J. Biol. Chem. 266:20791-20796(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
      Strain: Wistar.
      Tissue: Liver.
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Pituitary.
    3. "Three-dimensional structure of 6-pyruvoyl tetrahydropterin synthase, an enzyme involved in tetrahydrobiopterin biosynthesis."
      Nar H., Huber R., Heizmann C.W., Thoeny B., Buergisser D.
      EMBO J. 13:1255-1262(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
    4. "Crystallographic and kinetic investigations on the mechanism of 6-pyruvoyl tetrahydropterin synthase."
      Ploom T., Thoeny B., Yim J., Lee S., Nar H., Leimbacher W., Richardson J., Huber R., Auerbach G.
      J. Mol. Biol. 286:851-860(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).

    Entry informationi

    Entry nameiPTPS_RAT
    AccessioniPrimary (citable) accession number: P27213
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: August 1, 1992
    Last modified: October 1, 2014
    This is version 126 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The active site is at the interface between 2 subunits. The proton acceptor Cys is on one subunit, and the charge relay system is on the other subunit.

    Keywords - Technical termi

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

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3