P17276 · PH4H_DROME
- ProteinProtein henna
- GeneHn
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids452 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
Miscellaneous
In Drosophila, the 2 enzymes, PAH and TRH are found to be encoded by the same gene. Preference for the substrate is probably due to post-translational modifications such as phosphorylation, or by changes in the N-terminal regulatory domain.
Catalytic activity
- (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + L-phenylalanine + O2 = (4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin + L-tyrosine
Cofactor
Activity 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.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | iron ion binding | |
Molecular Function | phenylalanine 4-monooxygenase activity | |
Molecular Function | tryptophan 5-monooxygenase activity | |
Biological Process | dopamine biosynthetic process | |
Biological Process | eye pigment biosynthetic process | |
Biological Process | germ-band extension | |
Biological Process | L-phenylalanine catabolic process | |
Biological Process | long-term memory | |
Biological Process | serotonin biosynthetic process from tryptophan | |
Biological Process | tyrosine biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein henna
- EC number
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionP17276
- Secondary accessions
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000205552 | 1-452 | Protein henna | |||
Sequence: MYQRQVSFDKPTRVEDSAYIVEGVDIKEARNTCLLFSPKDSSLSSGALANILAIFKKHDINLVHIESRSSLRVPGYEFFVEADGKSGALGKAIEDVKEQCSYFNIISRDYKDNATAVPWFPRRIRDLDRFANQILSYGSELDADHPGFTDPEYRKRRKYFADIAYNYKHGEPLPHVDYTKEEIETWGIIFRNLTKLYKTHACREYNHVFPLLVDNCGFREDNIPQLEDVSNFLRDCTGFTLRPVAGLLSSRDFLAGLAFRVFHSTQYIRHPSKPMYTPEPDVCHELMGHVPLFADPAFAQFSQEIGLASLGAPDDYIEKLSTIFWFTVEYGVCRQEGELKAYGAGLLSSYGELEYCLTDKPQLKDFEPEVTGVTKYPITQFQPLYYVADSFETAKEKTIKFANSIPRPFGVRYNAYTQSVEVLDSKPQISNLMDNINSEFQILQNAVAKLRV | ||||||
Modified residue | 272 | Phosphoserine; by CaMK2 | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
Expression
Tissue specificity
Phenylalanine hydrolase activity is found in yolk granules of embryos, and female abdomen and fat body tissues. Tryptophan hydroxylase is expressed in serotonergic neurons. Both enzymes are present in cuticular tissues.
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 36-107 | ACT | ||||
Sequence: FSPKDSSLSSGALANILAIFKKHDINLVHIESRSSLRVPGYEFFVEADGKSGALGKAIEDVKEQCSYFNIIS |
Sequence similarities
Belongs to the biopterin-dependent aromatic amino acid hydroxylase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length452
- Mass (Da)51,660
- Last updated2000-12-01 v3
- Checksum990F554150056867
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 28 | in Ref. 2; AAA69513 | ||||
Sequence: E → A | ||||||
Sequence conflict | 39-47 | in Ref. 2; AAA69513 | ||||
Sequence: KDSSLSSGA → RIRRCPAEL | ||||||
Sequence conflict | 55-56 | in Ref. 2; AAA69513 | ||||
Sequence: FK → LR | ||||||
Sequence conflict | 63-71 | in Ref. 2; AAA69513 | ||||
Sequence: VHIESRSSL → CILSRILAPWF | ||||||
Sequence conflict | 74-114 | in Ref. 2; AAA69513 | ||||
Sequence: PGYEFFVEADGKSGALGKAIEDVKEQCSYFNIISRDYKDNA → SSCFWRRMENRSLGKSHRGCEGAMLATLTSSCRELQGVMP | ||||||
Sequence conflict | 154 | in Ref. 2; AAA69513 | ||||
Sequence: R → A | ||||||
Sequence conflict | 164 | in Ref. 2; AAA69513 | ||||
Sequence: A → G | ||||||
Sequence conflict | 171 | in Ref. 2; AAA69513 | ||||
Sequence: E → Q | ||||||
Sequence conflict | 264 | in Ref. 2; AAA69513 | ||||
Sequence: S → C | ||||||
Sequence conflict | 297 | in Ref. 2; AAA69513 | ||||
Sequence: A → S | ||||||
Sequence conflict | 332 | in Ref. 1; M81833 and 2; AAA69513 | ||||
Sequence: V → L | ||||||
Sequence conflict | 333-335 | in Ref. 2; AAA69513 | ||||
Sequence: CRQ → LAK | ||||||
Sequence conflict | 370 | in Ref. 2; AAA69513 | ||||
Sequence: V → S | ||||||
Sequence conflict | 449-452 | in Ref. 1; M81833 | ||||
Sequence: KLRV → NCASE |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M81833 EMBL· GenBank· DDBJ | - | Genomic RNA | No translation available. | |
M32802 EMBL· GenBank· DDBJ | AAA69513.1 EMBL· GenBank· DDBJ | mRNA | ||
X98116 EMBL· GenBank· DDBJ | CAA66797.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X98116 EMBL· GenBank· DDBJ | CAA66798.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014296 EMBL· GenBank· DDBJ | AAF50517.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY069306 EMBL· GenBank· DDBJ | AAL39451.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ001718 EMBL· GenBank· DDBJ | CAA04950.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ001719 EMBL· GenBank· DDBJ | CAB51601.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ001720 EMBL· GenBank· DDBJ | CAB51601.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ001722 EMBL· GenBank· DDBJ | CAB51599.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ001723 EMBL· GenBank· DDBJ | CAB51597.1 EMBL· GenBank· DDBJ | mRNA |