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Protein

Aromatic-L-amino-acid decarboxylase

Gene

Ddc

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine (DOPA) to dopamine, L-5-hydroxytryptophan to serotonin and L-tryptophan to tryptamine. Variation in the synthesis of bioamines may be a factor contributing to natural variation in life span.1 Publication

Catalytic activityi

L-dopa = dopamine + CO2.
5-hydroxy-L-tryptophan = 5-hydroxytryptamine + CO2.

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei117 – 1171SubstrateBy similarity
Binding sitei183 – 1831Pyridoxal phosphate; via amide nitrogenBy similarity
Binding sitei184 – 1841Pyridoxal phosphateBy similarity
Binding sitei227 – 2271SubstrateBy similarity
Binding sitei280 – 2801Pyridoxal phosphate; via carbonyl oxygenBy similarity
Binding sitei334 – 3341Pyridoxal phosphateBy similarity

GO - Molecular functioni

  • aromatic-L-amino-acid decarboxylase activity Source: FlyBase
  • pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  • adult chitin-containing cuticle pigmentation Source: FlyBase
  • anesthesia-resistant memory Source: FlyBase
  • catecholamine metabolic process Source: FlyBase
  • courtship behavior Source: FlyBase
  • developmental pigmentation Source: FlyBase
  • dopamine biosynthetic process from tyrosine Source: FlyBase
  • eclosion rhythm Source: FlyBase
  • growth Source: FlyBase
  • learning or memory Source: FlyBase
  • long-term memory Source: FlyBase
  • regulation of adult chitin-containing cuticle pigmentation Source: FlyBase
  • response to wounding Source: FlyBase
  • serotonin biosynthetic process from tryptophan Source: FlyBase
  • thermosensory behavior Source: FlyBase
  • thermotaxis Source: FlyBase
  • wing disc development Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Catecholamine biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BRENDAi4.1.1.28. 1994.
ReactomeiR-DME-209905. Catecholamine biosynthesis.
R-DME-209931. Serotonin and melatonin biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Aromatic-L-amino-acid decarboxylase (EC:4.1.1.28)
Short name:
AADC
Alternative name(s):
DOPA decarboxylase
Short name:
DDC
Gene namesi
Name:Ddc
ORF Names:CG10697
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0000422. Ddc.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 510510Aromatic-L-amino-acid decarboxylasePRO_0000146945Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei337 – 3371N6-(pyridoxal phosphate)lysineBy similarity

Proteomic databases

PaxDbiP05031.
PRIDEiP05031.

Expressioni

Tissue specificityi

Hypoderm isoform is expressed only in hypodermal epithelium and the CNS isoform only in central nervous system.2 Publications

Developmental stagei

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.2 Publications

Inductioni

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.1 Publication

Gene expression databases

BgeeiFBgn0000422.
ExpressionAtlasiP05031. differential.
GenevisibleiP05031. DM.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi61175. 2 interactions.
DIPiDIP-18733N.
IntActiP05031. 2 interactions.
MINTiMINT-812898.
STRINGi7227.FBpp0080710.

Structurei

Secondary structure

1
510
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi38 – 5720Combined sources
Helixi59 – 613Combined sources
Helixi74 – 763Combined sources
Helixi88 – 9811Combined sources
Helixi100 – 1023Combined sources
Helixi121 – 13313Combined sources
Beta strandi137 – 1393Combined sources
Helixi144 – 16017Combined sources
Helixi165 – 1673Combined sources
Helixi169 – 1713Combined sources
Beta strandi176 – 1816Combined sources
Helixi183 – 20523Combined sources
Helixi211 – 2177Combined sources
Beta strandi218 – 2236Combined sources
Helixi228 – 23710Combined sources
Beta strandi240 – 2445Combined sources
Helixi253 – 26513Combined sources
Beta strandi269 – 27810Combined sources
Turni280 – 2823Combined sources
Helixi288 – 29710Combined sources
Beta strandi301 – 3055Combined sources
Helixi309 – 3146Combined sources
Helixi316 – 3227Combined sources
Helixi325 – 3273Combined sources
Beta strandi329 – 3335Combined sources
Helixi335 – 3384Combined sources
Beta strandi346 – 3527Combined sources
Helixi353 – 3553Combined sources
Helixi387 – 3893Combined sources
Helixi391 – 42636Combined sources
Beta strandi430 – 4345Combined sources
Beta strandi440 – 4478Combined sources
Helixi449 – 46214Combined sources
Beta strandi468 – 4725Combined sources
Beta strandi475 – 4817Combined sources
Helixi489 – 50719Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3K40X-ray1.75A/B36-510[»]
ProteinModelPortaliP05031.
SMRiP05031. Positions 36-510.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05031.

Family & Domainsi

Sequence similaritiesi

Belongs to the group II decarboxylase family.Curated

Phylogenomic databases

eggNOGiKOG0628. Eukaryota.
COG0076. LUCA.
GeneTreeiENSGT00760000119205.
InParanoidiP05031.
KOiK01593.
OMAiNHRMRGA.
OrthoDBiEOG091G03KI.
PhylomeDBiP05031.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR010977. Aromatic_deC.
IPR002129. PyrdxlP-dep_de-COase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR021115. Pyridoxal-P_BS.
[Graphical view]
PfamiPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
PRINTSiPR00800. YHDCRBOXLASE.
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00392. DDC_GAD_HDC_YDC. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform CNS (identifier: P05031-1) [UniParc]FASTAAdd to basket
Also known as: Long, Brain, 56.7 kDa, C

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.

« Hide

        10         20         30         40         50
MSHIPISNTI PTKQTDGNGK ANISPDKLDP KVSIDMEAPE FKDFAKTMVD
60 70 80 90 100
FIAEYLENIR ERRVLPEVKP GYLKPLIPDA APEKPEKWQD VMQDIERVIM
110 120 130 140 150
PGVTHWHSPK FHAYFPTANS YPAIVADMLS GAIACIGFTW IASPACTELE
160 170 180 190 200
VVMMDWLGKM LELPAEFLAC SGGKGGGVIQ GTASESTLVA LLGAKAKKLK
210 220 230 240 250
EVKELHPEWD EHTILGKLVG YCSDQAHSSV ERAGLLGGVK LRSVQSENHR
260 270 280 290 300
MRGAALEKAI EQDVAEGLIP FYAVVTLGTT NSCAFDYLDE CGPVGNKHNL
310 320 330 340 350
WIHVDAAYAG SAFICPEYRH LMKGIESADS FNFNPHKWML VNFDCSAMWL
360 370 380 390 400
KDPSWVVNAF NVDPLYLKHD MQGSAPDYRH WQIPLGRRFR ALKLWFVLRL
410 420 430 440 450
YGVENLQAHI RRHCNFAKQF GDLCVADSRF ELAAEINMGL VCFRLKGSNE
460 470 480 490 500
RNEALLKRIN GRGHIHLVPA KIKDVYFLRM AICSRFTQSE DMEYSWKEVS
510
AAADEMEQEQ
Length:510
Mass (Da):57,288
Last modified:December 1, 2000 - v4
Checksum:i0A850488D407D4BF
GO
Isoform Hypoderm (identifier: P05031-2) [UniParc]FASTAAdd to basket
Also known as: Short, B, D

The sequence of this isoform differs from the canonical sequence as follows:
     1-35: Missing.

Show »
Length:475
Mass (Da):53,573
Checksum:iBFF4DB13EDF550A1
GO
Isoform 3 (identifier: P05031-3) [UniParc]FASTAAdd to basket
Also known as: Hypoderm, 56.2 kDa

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: MSHIPISNTIPTKQTDGNGKANISPDKLDPKVS → MSIGFRYRANNYARLITKYFCIHIK

Show »
Length:502
Mass (Da):56,863
Checksum:iD112AA488D6D02E9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti32 – 332Missing in CAB37087 (PubMed:3102230).Curated
Sequence conflicti479 – 4791R → A in CAB37087 (PubMed:3102230).Curated
Sequence conflicti479 – 4791R → A in CAB37088 (PubMed:3102230).Curated
Isoform 3 (identifier: P05031-3)
Sequence conflicti13 – 131A → V in AAO16848 (PubMed:12881721).Curated

Polymorphismi

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.1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti12 – 121T → P in allele Ddc-R6, allele Ddc-R9, allele Ddc-R16, allele Ddc-R20, allele Ddc-R25 and allele Ddc-R30. 1 Publication
Natural varianti197 – 1971K → N in allele Ddc-R9. 1 Publication
Natural varianti264 – 2641V → M in allele Ddc-R11 and allele Ddc-R18. 1 Publication
Natural varianti390 – 3901R → M in allele Ddc-Ore. 1 Publication
Natural varianti428 – 4281S → F in allele Ddc-R33. 1 Publication
Natural varianti489 – 4891S → A in allele Ddc-2b. 1 Publication

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3535Missing in isoform Hypoderm. CuratedVSP_001305Add
BLAST
Alternative sequencei1 – 3333MSHIP…DPKVS → MSIGFRYRANNYARLITKYF CIHIK in isoform 3. 1 PublicationVSP_001306Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04661 Genomic DNA. Translation: CAB37087.1.
X04661 Genomic DNA. Translation: CAB37088.1.
X04426 Genomic DNA. Translation: CAA28022.1.
X04426 Genomic DNA. Translation: CAA28023.1.
AY197756 Genomic DNA. Translation: AAO16831.1.
AY197756 Genomic DNA. Translation: AAO16832.1.
AY197757 Genomic DNA. Translation: AAO16833.1.
AY197757 Genomic DNA. Translation: AAO16834.1.
AY197758 Genomic DNA. Translation: AAO16835.1.
AY197758 Genomic DNA. Translation: AAO16836.1.
AY197759 Genomic DNA. Translation: AAO16837.1.
AY197759 Genomic DNA. Translation: AAO16838.1.
AY197760 Genomic DNA. Translation: AAO16839.1.
AY197760 Genomic DNA. Translation: AAO16840.1.
AY197761 Genomic DNA. Translation: AAO16841.1.
AY197761 Genomic DNA. Translation: AAO16842.1.
AY197762 Genomic DNA. Translation: AAO16843.1.
AY197762 Genomic DNA. Translation: AAO16844.1.
AY197763 Genomic DNA. Translation: AAO16845.1.
AY197763 Genomic DNA. Translation: AAO16846.1.
AY197764 Genomic DNA. Translation: AAO16847.1.
AY197764 Genomic DNA. Translation: AAO16848.1.
AY197765 Genomic DNA. Translation: AAO16849.1.
AY197765 Genomic DNA. Translation: AAO16850.1.
AY197766 Genomic DNA. Translation: AAO16851.1.
AY197766 Genomic DNA. Translation: AAO16852.1.
AY197767 Genomic DNA. Translation: AAO16853.1.
AY197767 Genomic DNA. Translation: AAO16854.1.
AY197768 Genomic DNA. Translation: AAO16855.1.
AY197768 Genomic DNA. Translation: AAO16856.1.
AY197769 Genomic DNA. Translation: AAO16857.1.
AY197769 Genomic DNA. Translation: AAO16858.1.
AE014134 Genomic DNA. Translation: AAF53762.1.
AE014134 Genomic DNA. Translation: AAF53763.1.
AE014134 Genomic DNA. Translation: AAF53764.3.
AY060708 mRNA. Translation: AAL28256.1.
AF091328 Genomic DNA. Translation: AAC67582.1.
X05991 Genomic DNA. Translation: CAA29409.2.
PIRiA25697. DCFFD1.
A25709. DCFFA.
B25697. DCFFD2.
RefSeqiNP_523600.5. NM_078876.5. [P05031-2]
NP_724163.1. NM_165279.2. [P05031-1]
NP_724164.1. NM_165280.2. [P05031-2]
UniGeneiDm.12979.

Genome annotation databases

EnsemblMetazoaiFBtr0081167; FBpp0080710; FBgn0000422. [P05031-1]
GeneIDi35190.
KEGGidme:Dmel_CG10697.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04661 Genomic DNA. Translation: CAB37087.1.
X04661 Genomic DNA. Translation: CAB37088.1.
X04426 Genomic DNA. Translation: CAA28022.1.
X04426 Genomic DNA. Translation: CAA28023.1.
AY197756 Genomic DNA. Translation: AAO16831.1.
AY197756 Genomic DNA. Translation: AAO16832.1.
AY197757 Genomic DNA. Translation: AAO16833.1.
AY197757 Genomic DNA. Translation: AAO16834.1.
AY197758 Genomic DNA. Translation: AAO16835.1.
AY197758 Genomic DNA. Translation: AAO16836.1.
AY197759 Genomic DNA. Translation: AAO16837.1.
AY197759 Genomic DNA. Translation: AAO16838.1.
AY197760 Genomic DNA. Translation: AAO16839.1.
AY197760 Genomic DNA. Translation: AAO16840.1.
AY197761 Genomic DNA. Translation: AAO16841.1.
AY197761 Genomic DNA. Translation: AAO16842.1.
AY197762 Genomic DNA. Translation: AAO16843.1.
AY197762 Genomic DNA. Translation: AAO16844.1.
AY197763 Genomic DNA. Translation: AAO16845.1.
AY197763 Genomic DNA. Translation: AAO16846.1.
AY197764 Genomic DNA. Translation: AAO16847.1.
AY197764 Genomic DNA. Translation: AAO16848.1.
AY197765 Genomic DNA. Translation: AAO16849.1.
AY197765 Genomic DNA. Translation: AAO16850.1.
AY197766 Genomic DNA. Translation: AAO16851.1.
AY197766 Genomic DNA. Translation: AAO16852.1.
AY197767 Genomic DNA. Translation: AAO16853.1.
AY197767 Genomic DNA. Translation: AAO16854.1.
AY197768 Genomic DNA. Translation: AAO16855.1.
AY197768 Genomic DNA. Translation: AAO16856.1.
AY197769 Genomic DNA. Translation: AAO16857.1.
AY197769 Genomic DNA. Translation: AAO16858.1.
AE014134 Genomic DNA. Translation: AAF53762.1.
AE014134 Genomic DNA. Translation: AAF53763.1.
AE014134 Genomic DNA. Translation: AAF53764.3.
AY060708 mRNA. Translation: AAL28256.1.
AF091328 Genomic DNA. Translation: AAC67582.1.
X05991 Genomic DNA. Translation: CAA29409.2.
PIRiA25697. DCFFD1.
A25709. DCFFA.
B25697. DCFFD2.
RefSeqiNP_523600.5. NM_078876.5. [P05031-2]
NP_724163.1. NM_165279.2. [P05031-1]
NP_724164.1. NM_165280.2. [P05031-2]
UniGeneiDm.12979.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3K40X-ray1.75A/B36-510[»]
ProteinModelPortaliP05031.
SMRiP05031. Positions 36-510.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi61175. 2 interactions.
DIPiDIP-18733N.
IntActiP05031. 2 interactions.
MINTiMINT-812898.
STRINGi7227.FBpp0080710.

Proteomic databases

PaxDbiP05031.
PRIDEiP05031.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0081167; FBpp0080710; FBgn0000422. [P05031-1]
GeneIDi35190.
KEGGidme:Dmel_CG10697.

Organism-specific databases

CTDi1644.
FlyBaseiFBgn0000422. Ddc.

Phylogenomic databases

eggNOGiKOG0628. Eukaryota.
COG0076. LUCA.
GeneTreeiENSGT00760000119205.
InParanoidiP05031.
KOiK01593.
OMAiNHRMRGA.
OrthoDBiEOG091G03KI.
PhylomeDBiP05031.

Enzyme and pathway databases

BRENDAi4.1.1.28. 1994.
ReactomeiR-DME-209905. Catecholamine biosynthesis.
R-DME-209931. Serotonin and melatonin biosynthesis.

Miscellaneous databases

ChiTaRSiDdc. fly.
EvolutionaryTraceiP05031.
GenomeRNAii35190.
PROiP05031.

Gene expression databases

BgeeiFBgn0000422.
ExpressionAtlasiP05031. differential.
GenevisibleiP05031. DM.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR010977. Aromatic_deC.
IPR002129. PyrdxlP-dep_de-COase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR021115. Pyridoxal-P_BS.
[Graphical view]
PfamiPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
PRINTSiPR00800. YHDCRBOXLASE.
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00392. DDC_GAD_HDC_YDC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDDC_DROME
AccessioniPrimary (citable) accession number: P05031
Secondary accession number(s): O18379
, P05032, Q24295, Q7YSJ0, Q7YSK5, Q7YSV6, Q7Z0E1, Q7Z0E2, Q7Z0E3, Q7Z0E4, Q7Z0E5, Q7Z0E6, Q7Z0E7, Q7Z0E8, Q7Z0E9, Q95SL9, Q9VIZ5, Q9VIZ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: December 1, 2000
Last modified: September 7, 2016
This is version 165 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.