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P04176

- PH4H_RAT

UniProt

P04176 - PH4H_RAT

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Protein

Phenylalanine-4-hydroxylase

Gene

Pah

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

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
Complete GO annotation...

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

        10         20         30         40         50
MAAVVLENGV LSRKLSDFGQ ETSYIEDNSN QNGAISLIFS LKEEVGALAK
60 70 80 90 100
VLRLFEENDI NLTHIESRPS RLNKDEYEFF TYLDKRTKPV LGSIIKSLRN
110 120 130 140 150
DIGATVHELS RDKEKNTVPW FPRTIQELDR FANQILSYGA ELDADHPGFK
160 170 180 190 200
DPVYRARRKQ FADIAYNYRH GQPIPRVEYT EEEKQTWGTV FRTLKALYKT
210 220 230 240 250
HACYEHNHIF PLLEKYCGFR EDNIPQLEDV SQFLQTCTGF RLRPVAGLLS
260 270 280 290 300
SRDFLGGLAF RVFHCTQYIR HGSKPMYTPE PDICHELLGH VPLFSDRSFA
310 320 330 340 350
QFSQEIGLAS LGAPDEYIEK LATIYWFTVE FGLCKEGDSI KAYGAGLLSS
360 370 380 390 400
FGELQYCLSD KPKLLPLELE KTACQEYSVT EFQPLYYVAE SFSDAKEKVR
410 420 430 440 450
TFAATIPRPF SVRYDPYTQR VEVLDNTQQL KILADSINSE VGILCNALQK

IKS
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