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P04176 (PH4H_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Phenylalanine-4-hydroxylase
Short name=PAH
EC=1.14.16.1
Alternative name(s):
Phe-4-monooxygenase
Gene names
Name:Pah
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length453 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Cofactor

Fe2+ ion.

Enzyme regulation

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.

Pathway

Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 1/6.

Subunit structure

Homodimer and homotetramer. Ref.4

Post-translational modification

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

Sequence similarities

Belongs to the biopterin-dependent aromatic amino acid hydroxylase family.

Contains 1 ACT domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 453452Phenylalanine-4-hydroxylase
PRO_0000205550

Regions

Domain36 – 11176ACT

Sites

Metal binding2851Iron
Metal binding2901Iron
Metal binding3301Iron

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue161Phosphoserine; by PKA Ref.2

Secondary structure

1 ................................................................. 453
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P04176 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 365D9E8A7E498D52

FASTA45351,822
        10         20         30         40         50         60 
MAAVVLENGV LSRKLSDFGQ ETSYIEDNSN QNGAISLIFS LKEEVGALAK VLRLFEENDI 

        70         80         90        100        110        120 
NLTHIESRPS RLNKDEYEFF TYLDKRTKPV LGSIIKSLRN DIGATVHELS RDKEKNTVPW 

       130        140        150        160        170        180 
FPRTIQELDR FANQILSYGA ELDADHPGFK DPVYRARRKQ FADIAYNYRH GQPIPRVEYT 

       190        200        210        220        230        240 
EEEKQTWGTV FRTLKALYKT HACYEHNHIF PLLEKYCGFR EDNIPQLEDV SQFLQTCTGF 

       250        260        270        280        290        300 
RLRPVAGLLS SRDFLGGLAF RVFHCTQYIR HGSKPMYTPE PDICHELLGH VPLFSDRSFA 

       310        320        330        340        350        360 
QFSQEIGLAS LGAPDEYIEK LATIYWFTVE FGLCKEGDSI KAYGAGLLSS FGELQYCLSD 

       370        380        390        400        410        420 
KPKLLPLELE KTACQEYSVT EFQPLYYVAE SFSDAKEKVR TFAATIPRPF SVRYDPYTQR 

       430        440        450 
VEVLDNTQQL KILADSINSE VGILCNALQK IKS

« Hide

References

[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]"Structural basis of autoregulation of phenylalanine hydroxylase."
Kobe B., Jennings I.G., House C.M., Michell B.J., Goodwill K.E., Santarsiero B.D., Stevens R.C., Cotton R.G., Kemp B.E.
Nat. Struct. Biol. 6:442-448(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M12337 mRNA. Translation: AAA41843.1.
K02599 mRNA. Translation: AAA41794.1.
IPIIPI00193258.
PIRWHRTF. A25321.
UniGeneRn.1652.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1PHZX-ray2.20A1-429[»]
2PHMX-ray2.60A1-429[»]
ProteinModelPortalP04176.
SMRP04176. Positions 19-427.
ModBaseSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000005844.

PTM databases

PhosphoSiteP04176.

Proteomic databases

PaxDbP04176.
PRIDEP04176.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCRGD:3248. rat.

Organism-specific databases

RGD3248. Pah.

Phylogenomic databases

eggNOGCOG3186.
HOGENOMHOG000233373.
HOVERGENHBG006841.
InParanoidP04176.
OrthoDBEOG4CNQR1.

Enzyme and pathway databases

SABIO-RKP04176.
UniPathwayUPA00139; UER00337.

Gene expression databases

ArrayExpressP04176.
GenevestigatorP04176.
GermOnlineENSRNOG00000004302. Rattus norvegicus.

Family and domain databases

Gene3D1.10.800.10. 1 hit.
InterProIPR002912. 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]
PANTHERPTHR11473. PTHR11473. 1 hit.
PfamPF01842. ACT. 1 hit.
PF00351. Biopterin_H. 1 hit.
[Graphical view]
PIRSFPIRSF000336. TH. 1 hit.
PRINTSPR00372. FYWHYDRXLASE.
SUPFAMSSF56534. Aaa_hydroxylase. 1 hit.
TIGRFAMsTIGR01268. Phe4hydrox_tetr. 1 hit.
PROSITEPS00367. BH4_AAA_HYDROXYL_1. 1 hit.
PS51410. BH4_AAA_HYDROXYL_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP04176.
ChEMBLCHEMBL3077.
EvolutionaryTraceP04176.

Entry information

Entry namePH4H_RAT
AccessionPrimary (citable) accession number: P04176
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: January 23, 2007
Last modified: April 3, 2013
This is version 128 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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