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Protein

Aromatic-L-amino-acid decarboxylase

Gene

DDC

Organism
Sus scrofa (Pig)
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.

Catalytic activityi

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

Cofactori

pyridoxal 5'-phosphate1 Publication

Pathwayi: dopamine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes dopamine from L-tyrosine.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Aromatic-L-amino-acid decarboxylase (DDC)
This subpathway is part of the pathway dopamine biosynthesis, which is itself part of Catecholamine biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes dopamine from L-tyrosine, the pathway dopamine biosynthesis and in Catecholamine biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei82 – 821Substrate
Binding sitei148 – 1481Pyridoxal phosphate; via amide nitrogenBy similarity
Binding sitei149 – 1491Pyridoxal phosphateBy similarity
Binding sitei192 – 1921Substrate
Binding sitei246 – 2461Pyridoxal phosphate; via carbonyl oxygenBy similarity
Binding sitei300 – 3001Pyridoxal phosphateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Catecholamine biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14992.
BRENDAi4.1.1.28. 6170.
UniPathwayiUPA00747; UER00734.

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
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2841.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 486486Aromatic-L-amino-acid decarboxylasePRO_0000146941Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei303 – 3031N6-(pyridoxal phosphate)lysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP80041.
PeptideAtlasiP80041.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000019955.

Chemistry

BindingDBiP80041.

Structurei

Secondary structure

1
486
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 2220Combined sources
Helixi24 – 263Combined sources
Helixi39 – 413Combined sources
Helixi53 – 6210Combined sources
Helixi65 – 673Combined sources
Beta strandi78 – 803Combined sources
Helixi86 – 9813Combined sources
Helixi105 – 1073Combined sources
Helixi109 – 12517Combined sources
Helixi130 – 1323Combined sources
Turni135 – 1373Combined sources
Beta strandi141 – 1466Combined sources
Helixi148 – 17023Combined sources
Helixi176 – 1827Combined sources
Beta strandi183 – 1886Combined sources
Helixi193 – 20210Combined sources
Beta strandi205 – 2095Combined sources
Helixi219 – 23113Combined sources
Beta strandi235 – 24410Combined sources
Turni246 – 2483Combined sources
Helixi254 – 26310Combined sources
Beta strandi267 – 2715Combined sources
Helixi275 – 2806Combined sources
Turni282 – 2843Combined sources
Helixi285 – 2884Combined sources
Helixi291 – 2933Combined sources
Beta strandi295 – 2995Combined sources
Helixi301 – 3044Combined sources
Beta strandi312 – 3176Combined sources
Helixi319 – 3235Combined sources
Helixi324 – 3263Combined sources
Helixi346 – 3483Combined sources
Beta strandi349 – 3513Combined sources
Helixi359 – 39436Combined sources
Beta strandi398 – 4003Combined sources
Beta strandi406 – 41510Combined sources
Helixi417 – 43014Combined sources
Beta strandi432 – 4343Combined sources
Beta strandi436 – 4405Combined sources
Beta strandi443 – 4497Combined sources
Helixi457 – 47519Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JS3X-ray2.25A/B1-486[»]
1JS6X-ray2.60A/B1-486[»]
ProteinModelPortaliP80041.
SMRiP80041. Positions 1-476.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80041.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati58 – 115581Add
BLAST
Repeati118 – 178612Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni58 – 1781212 X approximate tandem repeatsAdd
BLAST

Sequence similaritiesi

Belongs to the group II decarboxylase family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0628. Eukaryota.
COG0076. LUCA.
HOVERGENiHBG000944.
InParanoidiP80041.
KOiK01593.

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]

Sequencei

Sequence statusi: Complete.

P80041-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNASDFRRRG KEMVDYMADY LEGIEGRQVY PDVQPGYLRP LIPATAPQEP
60 70 80 90 100
DTFEDILQDV EKIIMPGVTH WHSPYFFAYF PTASSYPAML ADMLCGAIGC
110 120 130 140 150
IGFSWAASPA CTELETVMMD WLGKMLQLPE AFLAGEAGEG GGVIQGSASE
160 170 180 190 200
ATLVALLAAR TKVVRRLQAA SPGLTQGAVL EKLVAYASDQ AHSSVERAGL
210 220 230 240 250
IGGVKLKAIP SDGKFAMRAS ALQEALERDK AAGLIPFFVV ATLGTTSCCS
260 270 280 290 300
FDNLLEVGPI CHEEDIWLHV DAAYAGSAFI CPEFRHLLNG VEFADSFNFN
310 320 330 340 350
PHKWLLVNFD CSAMWVKRRT DLTGAFKLDP VYLKHSHQGS GLITDYRHWQ
360 370 380 390 400
LPLGRRFRSL KMWFVFRMYG VKGLQAYIRK HVQLSHEFEA FVLQDPRFEV
410 420 430 440 450
CAEVTLGLVC FRLKGSDGLN EALLERINSA RKIHLVPCRL RGQFVLRFAI
460 470 480
CSRKVESGHV RLAWEHIRGL AAELLAAEEG KAEIKS
Length:486
Mass (Da):53,936
Last modified:November 1, 1997 - v2
Checksum:i6CE5978531A9FFA4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S82290 mRNA. Translation: AAB47157.1.
PIRiS17848.
RefSeqiNP_999019.1. NM_213854.1.
UniGeneiSsc.6301.
Ssc.80654.

Genome annotation databases

GeneIDi396857.
KEGGissc:396857.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S82290 mRNA. Translation: AAB47157.1.
PIRiS17848.
RefSeqiNP_999019.1. NM_213854.1.
UniGeneiSsc.6301.
Ssc.80654.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JS3X-ray2.25A/B1-486[»]
1JS6X-ray2.60A/B1-486[»]
ProteinModelPortaliP80041.
SMRiP80041. Positions 1-476.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000019955.

Chemistry

BindingDBiP80041.
ChEMBLiCHEMBL2841.

Proteomic databases

PaxDbiP80041.
PeptideAtlasiP80041.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi396857.
KEGGissc:396857.

Organism-specific databases

CTDi1644.

Phylogenomic databases

eggNOGiKOG0628. Eukaryota.
COG0076. LUCA.
HOVERGENiHBG000944.
InParanoidiP80041.
KOiK01593.

Enzyme and pathway databases

UniPathwayiUPA00747; UER00734.
BioCyciMetaCyc:MONOMER-14992.
BRENDAi4.1.1.28. 6170.

Miscellaneous databases

EvolutionaryTraceiP80041.

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...

Publicationsi

  1. "Cloning and expression of pig kidney dopa decarboxylase: comparison of the naturally occurring and recombinant enzymes."
    Moore P.S., Dominici P., Borri-Voltattorni C.
    Biochem. J. 315:249-256(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Pig kidney 3,4-dihydroxyphenylalanine (dopa) decarboxylase. Primary structure and relationships to other amino acid decarboxylases."
    Maras B., Dominici P., Barra D., Bossa F., Borri-Voltattorni C.
    Eur. J. Biochem. 201:385-391(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-485, ACETYLATION AT MET-1.
    Tissue: Kidney.
  3. "Structural insight into Parkinson's disease treatment from drug-inhibited DOPA decarboxylase."
    Burkhard P., Dominici P., Borri-Voltattorni C., Jansonius J.N., Malashkevich V.N.
    Nat. Struct. Biol. 8:963-967(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE AND CARBIDOPA, COFACTOR, SUBUNIT.

Entry informationi

Entry nameiDDC_PIG
AccessioniPrimary (citable) accession number: P80041
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1997
Last modified: July 6, 2016
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, 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

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.