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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)DescriptionActionsGraphical viewLength
Binding sitei82Substrate1
Binding sitei148Pyridoxal phosphate; via amide nitrogenBy similarity1
Binding sitei149Pyridoxal phosphateBy similarity1
Binding sitei192Substrate1
Binding sitei246Pyridoxal phosphate; via carbonyl oxygenBy similarity1
Binding sitei300Pyridoxal phosphateBy similarity1

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 databases

ChEMBLiCHEMBL2841.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001469411 – 486Aromatic-L-amino-acid decarboxylaseAdd BLAST486

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionine1 Publication1
Modified residuei303N6-(pyridoxal phosphate)lysine1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP80041.
PeptideAtlasiP80041.
PRIDEiP80041.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000019955.

Chemistry databases

BindingDBiP80041.

Structurei

Secondary structure

1486
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 22Combined sources20
Helixi24 – 26Combined sources3
Helixi39 – 41Combined sources3
Helixi53 – 62Combined sources10
Helixi65 – 67Combined sources3
Beta strandi78 – 80Combined sources3
Helixi86 – 98Combined sources13
Helixi105 – 107Combined sources3
Helixi109 – 125Combined sources17
Helixi130 – 132Combined sources3
Turni135 – 137Combined sources3
Beta strandi141 – 146Combined sources6
Helixi148 – 170Combined sources23
Helixi176 – 182Combined sources7
Beta strandi183 – 188Combined sources6
Helixi193 – 202Combined sources10
Beta strandi205 – 209Combined sources5
Helixi219 – 231Combined sources13
Beta strandi235 – 244Combined sources10
Turni246 – 248Combined sources3
Helixi254 – 263Combined sources10
Beta strandi267 – 271Combined sources5
Helixi275 – 280Combined sources6
Turni282 – 284Combined sources3
Helixi285 – 288Combined sources4
Helixi291 – 293Combined sources3
Beta strandi295 – 299Combined sources5
Helixi301 – 304Combined sources4
Beta strandi312 – 317Combined sources6
Helixi319 – 323Combined sources5
Helixi324 – 326Combined sources3
Helixi346 – 348Combined sources3
Beta strandi349 – 351Combined sources3
Helixi359 – 394Combined sources36
Beta strandi398 – 400Combined sources3
Beta strandi406 – 415Combined sources10
Helixi417 – 430Combined sources14
Beta strandi432 – 434Combined sources3
Beta strandi436 – 440Combined sources5
Beta strandi443 – 449Combined sources7
Helixi457 – 475Combined sources19

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP80041.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati58 – 1151Add BLAST58
Repeati118 – 1782Add BLAST61

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni58 – 1782 X approximate tandem repeatsAdd BLAST121

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JS3X-ray2.25A/B1-486[»]
1JS6X-ray2.60A/B1-486[»]
ProteinModelPortaliP80041.
SMRiP80041.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000019955.

Chemistry databases

BindingDBiP80041.
ChEMBLiCHEMBL2841.

Proteomic databases

PaxDbiP80041.
PeptideAtlasiP80041.
PRIDEiP80041.

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...

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: November 2, 2016
This is version 110 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.