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P04176

- PH4H_RAT

UniProt

P04176 - PH4H_RAT

Protein

Phenylalanine-4-hydroxylase

Gene

Pah

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    L-phenylalanine + tetrahydrobiopterin + O2 = L-tyrosine + 4a-hydroxytetrahydrobiopterin.

    Cofactori

    Fe2+ ion.

    Enzyme regulationi

    N-terminal region of PAH is thought to contain allosteric binding sites for phenylalanine and to constitute an "inhibitory" domain that regulates the activity of a catalytic domain in the C-terminal portion of the molecule.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi285 – 2851Iron
    Metal bindingi290 – 2901Iron
    Metal bindingi330 – 3301Iron

    GO - Molecular functioni

    1. amino acid binding Source: RGD
    2. cofactor binding Source: RGD
    3. iron ion binding Source: RGD
    4. phenylalanine 4-monooxygenase activity Source: RGD
    5. protein homodimerization activity Source: RGD

    GO - Biological processi

    1. L-phenylalanine catabolic process Source: UniProtKB-UniPathway
    2. L-phenylalanine metabolic process Source: RGD
    3. protein hydroxylation Source: RGD
    4. pteridine-containing compound metabolic process Source: RGD
    5. tetrahydrobiopterin metabolic process Source: RGD
    6. tyrosine biosynthetic process Source: RGD

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Biological processi

    Phenylalanine catabolism

    Keywords - Ligandi

    Iron, Metal-binding

    Enzyme and pathway databases

    SABIO-RKP04176.
    UniPathwayiUPA00139; UER00337.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phenylalanine-4-hydroxylase (EC:1.14.16.1)
    Short name:
    PAH
    Alternative name(s):
    Phe-4-monooxygenase
    Gene namesi
    Name:Pah
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi3248. Pah.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 453452Phenylalanine-4-hydroxylasePRO_0000205550Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei16 – 161Phosphoserine; by PKA1 Publication

    Post-translational modificationi

    Phosphorylation at Ser-16 increases basal activity and facilitates activation by the substrate phenylalanine.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiP04176.
    PRIDEiP04176.

    PTM databases

    PhosphoSiteiP04176.

    Expressioni

    Gene expression databases

    GenevestigatoriP04176.

    Interactioni

    Subunit structurei

    Homodimer and homotetramer.1 Publication

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000005844.

    Structurei

    Secondary structure

    1
    453
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi35 – 428
    Helixi47 – 5610
    Turni57 – 593
    Beta strandi64 – 696
    Beta strandi76 – 816
    Helixi85 – 873
    Helixi88 – 10013
    Beta strandi106 – 1105
    Helixi125 – 1295
    Turni130 – 1334
    Turni147 – 1504
    Helixi152 – 16615
    Helixi181 – 20121
    Helixi204 – 21613
    Helixi227 – 23812
    Beta strandi241 – 2444
    Helixi251 – 2588
    Turni259 – 2613
    Beta strandi262 – 2654
    Helixi283 – 2897
    Helixi291 – 2944
    Helixi297 – 31014
    Helixi315 – 32612
    Turni327 – 3315
    Beta strandi333 – 3364
    Beta strandi339 – 3424
    Helixi345 – 3484
    Helixi351 – 3577
    Beta strandi359 – 3668
    Helixi369 – 3724
    Beta strandi379 – 3824
    Beta strandi384 – 3907
    Helixi392 – 40312
    Beta strandi409 – 4157
    Turni416 – 4194
    Beta strandi420 – 4245

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1PHZX-ray2.20A1-429[»]
    2PHMX-ray2.60A1-429[»]
    ProteinModelPortaliP04176.
    SMRiP04176. Positions 19-427.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP04176.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini36 – 11479ACTPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 ACT domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG3186.
    HOGENOMiHOG000233373.
    HOVERGENiHBG006841.
    InParanoidiP04176.
    PhylomeDBiP04176.

    Family and domain databases

    Gene3Di1.10.800.10. 1 hit.
    InterProiIPR002912. ACT_dom.
    IPR001273. ArAA_hydroxylase.
    IPR018301. ArAA_hydroxylase_Fe/CU_BS.
    IPR019774. Aromatic-AA_hydroxylase_C.
    IPR005961. Phe-4-hydroxylase_tetra.
    IPR019773. Tyrosine_3-monooxygenase-like.
    [Graphical view]
    PANTHERiPTHR11473. PTHR11473. 1 hit.
    PfamiPF01842. ACT. 1 hit.
    PF00351. Biopterin_H. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000336. TH. 1 hit.
    PRINTSiPR00372. FYWHYDRXLASE.
    SUPFAMiSSF56534. SSF56534. 1 hit.
    TIGRFAMsiTIGR01268. Phe4hydrox_tetr. 1 hit.
    PROSITEiPS51671. ACT. 1 hit.
    PS00367. BH4_AAA_HYDROXYL_1. 1 hit.
    PS51410. BH4_AAA_HYDROXYL_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P04176-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAVVLENGV LSRKLSDFGQ ETSYIEDNSN QNGAISLIFS LKEEVGALAK    50
    VLRLFEENDI NLTHIESRPS RLNKDEYEFF TYLDKRTKPV LGSIIKSLRN 100
    DIGATVHELS RDKEKNTVPW FPRTIQELDR FANQILSYGA ELDADHPGFK 150
    DPVYRARRKQ FADIAYNYRH GQPIPRVEYT EEEKQTWGTV FRTLKALYKT 200
    HACYEHNHIF PLLEKYCGFR EDNIPQLEDV SQFLQTCTGF RLRPVAGLLS 250
    SRDFLGGLAF RVFHCTQYIR HGSKPMYTPE PDICHELLGH VPLFSDRSFA 300
    QFSQEIGLAS LGAPDEYIEK LATIYWFTVE FGLCKEGDSI KAYGAGLLSS 350
    FGELQYCLSD KPKLLPLELE KTACQEYSVT EFQPLYYVAE SFSDAKEKVR 400
    TFAATIPRPF SVRYDPYTQR VEVLDNTQQL KILADSINSE VGILCNALQK 450
    IKS 453
    Length:453
    Mass (Da):51,822
    Last modified:January 23, 2007 - v3
    Checksum:i365D9E8A7E498D52
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M12337 mRNA. Translation: AAA41843.1.
    K02599 mRNA. Translation: AAA41794.1.
    PIRiA25321. WHRTF.
    UniGeneiRn.1652.

    Genome annotation databases

    UCSCiRGD:3248. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M12337 mRNA. Translation: AAA41843.1 .
    K02599 mRNA. Translation: AAA41794.1 .
    PIRi A25321. WHRTF.
    UniGenei Rn.1652.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1PHZ X-ray 2.20 A 1-429 [» ]
    2PHM X-ray 2.60 A 1-429 [» ]
    ProteinModelPortali P04176.
    SMRi P04176. Positions 19-427.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000005844.

    Chemistry

    BindingDBi P04176.
    ChEMBLi CHEMBL3077.
    GuidetoPHARMACOLOGYi 1240.

    PTM databases

    PhosphoSitei P04176.

    Proteomic databases

    PaxDbi P04176.
    PRIDEi P04176.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    UCSCi RGD:3248. rat.

    Organism-specific databases

    RGDi 3248. Pah.

    Phylogenomic databases

    eggNOGi COG3186.
    HOGENOMi HOG000233373.
    HOVERGENi HBG006841.
    InParanoidi P04176.
    PhylomeDBi P04176.

    Enzyme and pathway databases

    UniPathwayi UPA00139 ; UER00337 .
    SABIO-RK P04176.

    Miscellaneous databases

    EvolutionaryTracei P04176.

    Gene expression databases

    Genevestigatori P04176.

    Family and domain databases

    Gene3Di 1.10.800.10. 1 hit.
    InterProi IPR002912. ACT_dom.
    IPR001273. ArAA_hydroxylase.
    IPR018301. ArAA_hydroxylase_Fe/CU_BS.
    IPR019774. Aromatic-AA_hydroxylase_C.
    IPR005961. Phe-4-hydroxylase_tetra.
    IPR019773. Tyrosine_3-monooxygenase-like.
    [Graphical view ]
    PANTHERi PTHR11473. PTHR11473. 1 hit.
    Pfami PF01842. ACT. 1 hit.
    PF00351. Biopterin_H. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000336. TH. 1 hit.
    PRINTSi PR00372. FYWHYDRXLASE.
    SUPFAMi SSF56534. SSF56534. 1 hit.
    TIGRFAMsi TIGR01268. Phe4hydrox_tetr. 1 hit.
    PROSITEi PS51671. ACT. 1 hit.
    PS00367. BH4_AAA_HYDROXYL_1. 1 hit.
    PS51410. BH4_AAA_HYDROXYL_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and sequence of a cDNA clone which contains the complete coding region of rat phenylalanine hydroxylase. Structural homology with tyrosine hydroxylase, glucocorticoid regulation, and use of alternate polyadenylation sites."
      Dahl H.-H.M., Mercer J.F.B.
      J. Biol. Chem. 261:4148-4153(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Amino acid sequence at the phosphorylated site of rat liver phenylalanine hydroxylase and phosphorylation of a corresponding synthetic peptide."
      Wretborn M., Humble E., Ragnarsson U., Engstrom L.
      Biochem. Biophys. Res. Commun. 93:403-408(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 12-21, PHOSPHORYLATION AT SER-16.
      Tissue: Liver.
    3. "Sequence comparison of rat liver phenylalanine hydroxylase and its cDNA clones."
      Robson K.J.H., Beattie W., James R.J., Cotton R.C.H., Morgan F.J., Woo S.L.C.
      Biochemistry 23:5671-5675(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 208-453.
    4. "Purification and characterization of phenylalanine 4-monooxygenase from rat liver."
      Nakata H., Fujisawa H.
      Biochim. Biophys. Acta 614:313-327(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    5. Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).

    Entry informationi

    Entry nameiPH4H_RAT
    AccessioniPrimary (citable) accession number: P04176
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 20, 1987
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 138 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Allosteric enzyme, 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