P05031 · DDC_DROME
- ProteinAromatic-L-amino-acid decarboxylase
- GeneDdc
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids510 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Isoform Hypoderm
Catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine (L-DOPA) to dopamine and L-5-hydroxytryptophan (5-HTP) to serotonin (PubMed:20098687).
Catalyzes the formation of serotonin more efficiently than dopamine (PubMed:20098687).
Displays no activity to tyrosine (PubMed:20098687).
Variation in the synthesis of bioamines may be a factor contributing to natural variation in life span (PubMed:12881721).
Catalyzes the formation of serotonin more efficiently than dopamine (PubMed:20098687).
Displays no activity to tyrosine (PubMed:20098687).
Variation in the synthesis of bioamines may be a factor contributing to natural variation in life span (PubMed:12881721).
Catalytic activity
Isoform Hypoderm
H+ + L-dopa = CO2 + dopamineThis reaction proceeds in the forward direction.Isoform Hypoderm
5-hydroxy-L-tryptophan + H+ = CO2 + serotonin
Cofactor
Isoform Hypoderm
pyridoxal 5'-phosphate (UniProtKB | Rhea| CHEBI:597326 )Kinetics
Isoform Hypoderm
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
1.26 mM | L-dopa | |||||
2.2 mM | L-Dopa | |||||
0.4 mM | 5-HTP |
pH Dependence
Optimum pH is 7.
Temperature Dependence
Optimum temperature is 30-60 degrees Celsius.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 117 | substrate | ||||
Sequence: T | ||||||
Binding site | 183 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 184 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Active site | 227 | |||||
Sequence: H | ||||||
Binding site | 227 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 227 | substrate | ||||
Sequence: H | ||||||
Binding site | 305 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 334 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: N |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | 5-hydroxy-L-tryptophan decarboxylase activity | |
Molecular Function | aromatic-L-amino-acid decarboxylase activity | |
Molecular Function | L-dopa decarboxylase activity | |
Molecular Function | pyridoxal phosphate binding | |
Biological Process | adult chitin-containing cuticle pigmentation | |
Biological Process | anesthesia-resistant memory | |
Biological Process | catecholamine metabolic process | |
Biological Process | dopamine biosynthetic process from tyrosine | |
Biological Process | long-term memory | |
Biological Process | regulation of adult chitin-containing cuticle pigmentation | |
Biological Process | response to hydrogen peroxide | |
Biological Process | response to wounding | |
Biological Process | serotonin biosynthetic process | |
Biological Process | serotonin biosynthetic process from tryptophan | |
Biological Process | thermosensory behavior | |
Biological Process | thermotaxis | |
Biological Process | wing disc development |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAromatic-L-amino-acid decarboxylase
- EC number
- Short namesAADC
- 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 accessionP05031
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Disruption phenotype
Simultaneous knockdown of Ddc and myc restores increased dopamine levels and the induced male-male courtship observed in the single myc knockdown.
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 12 | in allele Ddc-R6, allele Ddc-R9, allele Ddc-R16, allele Ddc-R20, allele Ddc-R25 and allele Ddc-R30 | ||||
Sequence: T → P | ||||||
Mutagenesis | 117 | Decreased specific activity to L-DOPA. Increased specific activity to 5-HTP. Decreased ligand binding affinity. | ||||
Sequence: T → A | ||||||
Mutagenesis | 117 | Increased specific activity to L-DOPA and 5-HTP. Decreased ligand binding affinity. | ||||
Sequence: T → S | ||||||
Natural variant | 197 | in allele Ddc-R9 | ||||
Sequence: K → N | ||||||
Mutagenesis | 227 | Enzymatic shift from L-dopa decarboxylation of to L-Dopa decarboxylation-oxidative deamination. | ||||
Sequence: H → N | ||||||
Mutagenesis | 227 | Decreased specific activity to L-DOPA and 5-HTP. Decreased ligand binding affinity. | ||||
Sequence: H → W | ||||||
Natural variant | 264 | in allele Ddc-R11 and allele Ddc-R18 | ||||
Sequence: V → M | ||||||
Natural variant | 390 | in allele Ddc-Ore | ||||
Sequence: R → M | ||||||
Natural variant | 428 | in allele Ddc-R33 | ||||
Sequence: S → F | ||||||
Natural variant | 489 | in allele Ddc-2b | ||||
Sequence: S → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 6 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000146945 | 1-510 | Aromatic-L-amino-acid decarboxylase | |||
Sequence: MSHIPISNTIPTKQTDGNGKANISPDKLDPKVSIDMEAPEFKDFAKTMVDFIAEYLENIRERRVLPEVKPGYLKPLIPDAAPEKPEKWQDVMQDIERVIMPGVTHWHSPKFHAYFPTANSYPAIVADMLSGAIACIGFTWIASPACTELEVVMMDWLGKMLELPAEFLACSGGKGGGVIQGTASESTLVALLGAKAKKLKEVKELHPEWDEHTILGKLVGYCSDQAHSSVERAGLLGGVKLRSVQSENHRMRGAALEKAIEQDVAEGLIPFYAVVTLGTTNSCAFDYLDECGPVGNKHNLWIHVDAAYAGSAFICPEYRHLMKGIESADSFNFNPHKWMLVNFDCSAMWLKDPSWVVNAFNVDPLYLKHDMQGSAPDYRHWQIPLGRRFRALKLWFVLRLYGVENLQAHIRRHCNFAKQFGDLCVADSRFELAAEINMGLVCFRLKGSNERNEALLKRINGRGHIHLVPAKIKDVYFLRMAICSRFTQSEDMEYSWKEVSAAADEMEQEQ | ||||||
Modified residue | 337 | N6-(pyridoxal phosphate)lysine | ||||
Sequence: K |
Proteomic databases
Expression
Tissue specificity
Hypoderm isoform is expressed only in hypodermal epithelium and the CNS isoform only in central nervous system. Expressed in the adult head (at protein level) (PubMed:35167135).
Induction
By ecdysone. In larval epidermis, expression is rapidly induced. In adult epidermis expression responds to a pulse of hormone and there is a time lag between initial exposure and appearance of DDC.
Developmental stage
Hypoderm isoform has high expression levels in hypoderm during late embryogenesis, late larval development, pupariation and adult eclosion. CNS isoform has constant expression level in CNS throughout the life cycle.
Gene expression databases
Structure
Family & Domains
Features
Showing features for compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-21 | Polar residues | ||||
Sequence: MSHIPISNTIPTKQTDGNGKA | ||||||
Region | 1-28 | Disordered | ||||
Sequence: MSHIPISNTIPTKQTDGNGKANISPDKL | ||||||
Region | 358-384 | Disordered | ||||
Sequence: NAFNVDPLYLKHDMQGSAPDYRHWQIP |
Sequence similarities
Belongs to the group II decarboxylase family.
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
P05031-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- NameCNS
- SynonymsLong, Brain, 56.7 kDa, C
- Length510
- Mass (Da)57,288
- Last updated2000-12-01 v4
- Checksum0A850488D407D4BF
P05031-2
- NameHypoderm
- SynonymsShort, B, D
- Differences from canonical
- 1-35: Missing
P05031-3
- Name3
- SynonymsHypoderm, 56.2 kDa
- Differences from canonical
- 1-33: MSHIPISNTIPTKQTDGNGKANISPDKLDPKVS → MSIGFRYRANNYARLITKYFCIHIK
Features
Showing features for compositional bias, alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-21 | Polar residues | ||||
Sequence: MSHIPISNTIPTKQTDGNGKA | ||||||
Alternative sequence | VSP_001306 | 1-33 | in isoform 3 | |||
Sequence: MSHIPISNTIPTKQTDGNGKANISPDKLDPKVS → MSIGFRYRANNYARLITKYFCIHIK | ||||||
Alternative sequence | VSP_001305 | 1-35 | in isoform Hypoderm | |||
Sequence: Missing | ||||||
Sequence conflict | 13 | In isoform P05031-3; in Ref. 4; AAO16848 | ||||
Sequence: A → V | ||||||
Sequence conflict | 32-33 | in Ref. 1; CAB37087 | ||||
Sequence: Missing | ||||||
Sequence conflict | 479 | in Ref. 1; CAB37087/CAB37088 | ||||
Sequence: R → A |
Polymorphism
Three common molecular polymorphisms (2 in the promoter region and Phe-12) account for 15.5% of the genetic contribution to variance in life span, the polymorphisms are maintained by balancing selection.
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X04661 EMBL· GenBank· DDBJ | CAB37087.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X04661 EMBL· GenBank· DDBJ | CAB37088.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X04426 EMBL· GenBank· DDBJ | CAA28022.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X04426 EMBL· GenBank· DDBJ | CAA28023.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY197756 EMBL· GenBank· DDBJ | AAO16831.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY197756 EMBL· GenBank· DDBJ | AAO16832.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY197757 EMBL· GenBank· DDBJ | AAO16833.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY197757 EMBL· GenBank· DDBJ | AAO16834.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY197758 EMBL· GenBank· DDBJ | AAO16835.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY197758 EMBL· GenBank· DDBJ | AAO16836.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY197759 EMBL· GenBank· DDBJ | AAO16837.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY197759 EMBL· GenBank· DDBJ | AAO16838.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY197760 EMBL· GenBank· DDBJ | AAO16839.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY197760 EMBL· GenBank· DDBJ | AAO16840.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY197761 EMBL· GenBank· DDBJ | AAO16841.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY197761 EMBL· GenBank· DDBJ | AAO16842.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY197762 EMBL· GenBank· DDBJ | AAO16843.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY197762 EMBL· GenBank· DDBJ | AAO16844.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY197763 EMBL· GenBank· DDBJ | AAO16845.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY197763 EMBL· GenBank· DDBJ | AAO16846.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY197764 EMBL· GenBank· DDBJ | AAO16847.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY197764 EMBL· GenBank· DDBJ | AAO16848.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY197765 EMBL· GenBank· DDBJ | AAO16849.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY197765 EMBL· GenBank· DDBJ | AAO16850.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY197766 EMBL· GenBank· DDBJ | AAO16851.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY197766 EMBL· GenBank· DDBJ | AAO16852.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY197767 EMBL· GenBank· DDBJ | AAO16853.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY197767 EMBL· GenBank· DDBJ | AAO16854.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY197768 EMBL· GenBank· DDBJ | AAO16855.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY197768 EMBL· GenBank· DDBJ | AAO16856.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY197769 EMBL· GenBank· DDBJ | AAO16857.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY197769 EMBL· GenBank· DDBJ | AAO16858.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014134 EMBL· GenBank· DDBJ | AAF53762.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014134 EMBL· GenBank· DDBJ | AAF53763.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014134 EMBL· GenBank· DDBJ | AAF53764.3 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY060708 EMBL· GenBank· DDBJ | AAL28256.1 EMBL· GenBank· DDBJ | mRNA | ||
AF091328 EMBL· GenBank· DDBJ | AAC67582.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X05991 EMBL· GenBank· DDBJ | CAA29409.2 EMBL· GenBank· DDBJ | Genomic DNA |