Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Aromatic-L-amino-acid decarboxylase

Gene

Ddc

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -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. Tyrosine 3-monooxygenase (Th)
  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 sitei82SubstrateBy similarity1
Binding sitei148Pyridoxal phosphate; via amide nitrogenBy similarity1
Binding sitei149Pyridoxal phosphateBy similarity1
Binding sitei192SubstrateBy similarity1
Binding sitei246Pyridoxal phosphate; via carbonyl oxygenBy similarity1
Binding sitei300Pyridoxal phosphateBy similarity1

GO - Molecular functioni

  • amino acid binding Source: RGD
  • aromatic-L-amino-acid decarboxylase activity Source: RGD
  • enzyme binding Source: Ensembl
  • L-dopa decarboxylase activity Source: Ensembl
  • protein domain specific binding Source: RGD
  • pyridoxal phosphate binding Source: RGD

GO - Biological processi

  • aminergic neurotransmitter loading into synaptic vesicle Source: RGD
  • catecholamine biosynthetic process Source: RGD
  • cellular amino acid metabolic process Source: InterPro
  • cellular response to alkaloid Source: RGD
  • cellular response to drug Source: RGD
  • cellular response to growth factor stimulus Source: RGD
  • circadian rhythm Source: RGD
  • dopamine biosynthetic process Source: RGD
  • dopamine metabolic process Source: RGD
  • isoquinoline alkaloid metabolic process Source: RGD
  • multicellular organism aging Source: RGD
  • phytoalexin metabolic process Source: RGD
  • response to pyrethroid Source: RGD
  • serotonin biosynthetic process Source: RGD

Keywordsi

Molecular functionDecarboxylase, Lyase
Biological processCatecholamine biosynthesis
LigandPyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15070
ReactomeiR-RNO-209905 Catecholamine biosynthesis
R-RNO-209931 Serotonin and melatonin biosynthesis
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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 14

Organism-specific databases

RGDi2494 Ddc

Subcellular locationi

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi192H → A: Abolishes decarboxylase activity. 2 Publications1
Mutagenesisi192H → Q: Reduces decarboxylase activity by 96%. 2 Publications1
Mutagenesisi252D → A or E: Abolishes decarboxylase activity. 1 Publication1
Mutagenesisi271D → A: Abolishes decarboxylase activity. 2 Publications1
Mutagenesisi271D → E: Reduces decarboxylase activity by 65%. 2 Publications1
Mutagenesisi296S → A: Abolishes decarboxylase activity. 1 Publication1
Mutagenesisi300N → A: Reduces decarboxylase activity by 75%. 1 Publication1
Mutagenesisi302H → Q: Reduces decarboxylase activity by 99.8%. 1 Publication1
Mutagenesisi303K → A or R: Abolishes decarboxylase activity. 1 Publication1
Mutagenesisi332Y → A or F: Abolishes decarboxylase activity. 1 Publication1
Mutagenesisi355R → A: Abolishes decarboxylase activity. 1 Publication1
Mutagenesisi355R → K: No effect. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001469421 – 480Aromatic-L-amino-acid decarboxylaseAdd BLAST480

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei303N6-(pyridoxal phosphate)lysine1

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP14173
PRIDEiP14173

PTM databases

iPTMnetiP14173
PhosphoSitePlusiP14173

Expressioni

Gene expression databases

BgeeiENSRNOG00000004327
ExpressionAtlasiP14173 baseline and differential
GenevisibleiP14173 RN

Interactioni

Subunit structurei

Homodimer.

GO - Molecular functioni

  • enzyme binding Source: Ensembl
  • protein domain specific binding Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000064520

Structurei

3D structure databases

ProteinModelPortaliP14173
SMRiP14173
ModBaseiSearch...
MobiDBiSearch...

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
GeneTreeiENSGT00760000119205
HOVERGENiHBG000944
InParanoidiP14173
KOiK01593
OMAiSAMWVKK
OrthoDBiEOG091G03KI
PhylomeDBiP14173
TreeFamiTF313863

Family and domain databases

Gene3Di3.40.640.10, 1 hit
3.90.1150.10, 1 hit
InterProiView protein in InterPro
IPR010977 Aromatic_deC
IPR002129 PyrdxlP-dep_de-COase
IPR015424 PyrdxlP-dep_Trfase
IPR015422 PyrdxlP-dep_Trfase_dom1
IPR015421 PyrdxlP-dep_Trfase_major
IPR021115 Pyridoxal-P_BS
PfamiView protein in Pfam
PF00282 Pyridoxal_deC, 1 hit
PRINTSiPR00800 YHDCRBOXLASE
SUPFAMiSSF53383 SSF53383, 1 hit
PROSITEiView protein in PROSITE
PS00392 DDC_GAD_HDC_YDC, 1 hit

Sequencei

Sequence statusi: Complete.

P14173-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDSREFRRRG KEMVDYIADY LDGIEGRPVY PDVEPGYLRA LIPTTAPQEP
60 70 80 90 100
ETYEDIIRDI EKIIMPGVTH WHSPYFFAYF PTASSYPAML ADMLCGAIGC
110 120 130 140 150
IGFSWAASPA CTELETVMMD WLGKMLELPE AFLAGRAGEG GGVIQGSASE
160 170 180 190 200
ATLVALLAAR TKMIRQLQAA SPELTQAALM EKLVAYTSDQ AHSSVERAGL
210 220 230 240 250
IGGVKIKAIP SDGNYSMRAA ALREALERDK AAGLIPFFVV VTLGTTSCCS
260 270 280 290 300
FDNLLEVGPI CNQEGVWLHI DAAYAGSAFI CPEFRYLLNG VEFADSFNFN
310 320 330 340 350
PHKWLLVNFD CSAMWVKKRT DLTEAFNMDP VYLRHSHQDS GLITDYRHWQ
360 370 380 390 400
IPLGRRFRSL KMWFVFRMYG VKGLQAYIRK HVKLSHEFES LVRQDPRFEI
410 420 430 440 450
CTEVILGLVC FRLKGSNQLN ETLLQRINSA KKIHLVPCRL RDKFVLRFAV
460 470 480
CSRTVESAHV QLAWEHIRDL ASSVLRAEKE
Length:480
Mass (Da):54,053
Last modified:January 1, 1990 - v1
Checksum:i1E1D077488704574
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L33001
, L32989, L32990, L32991, L32992, L32993, L32994, L32995, L32996, L32997, L33003, L32999, L33000 Genomic DNA Translation: AAA40646.1
M27716 mRNA Translation: AAA41087.1
BC087032 mRNA Translation: AAH87032.1
L03417 Genomic DNA Translation: AAA99905.1
PIRiA33994 DCRTA
RefSeqiNP_001257781.1, NM_001270852.1
NP_001257782.1, NM_001270853.1
NP_036677.1, NM_012545.4
XP_006251537.1, XM_006251475.3
XP_008768474.1, XM_008770252.2
UniGeneiRn.11064

Genome annotation databases

EnsembliENSRNOT00000005851; ENSRNOP00000005851; ENSRNOG00000004327
ENSRNOT00000073892; ENSRNOP00000064520; ENSRNOG00000004327
GeneIDi24311
KEGGirno:24311
UCSCiRGD:2494 rat

Similar proteinsi

Entry informationi

Entry nameiDDC_RAT
AccessioniPrimary (citable) accession number: P14173
Secondary accession number(s): Q6LEG4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: June 20, 2018
This is version 148 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health