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Protein

Aromatic-L-amino-acid decarboxylase

Gene

Ddc

Organism
Rattus norvegicus (Rat)
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

Sites

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

GO - Molecular functioni

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

GO - Biological processi

  • 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 organismal aging Source: RGD
  • phytoalexin metabolic process Source: RGD
  • response to pyrethroid Source: RGD
  • serotonin biosynthetic process Source: RGD
  • synaptic vesicle amine transport Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Catecholamine biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15070.
ReactomeiREACT_295841. Catecholamine biosynthesis.
REACT_336165. 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 14

Organism-specific databases

RGDi2494. Ddc.

Subcellular locationi

GO - Cellular componenti

  • axon Source: RGD
  • cytoplasm Source: RGD
  • extracellular exosome Source: Ensembl
  • intracellular Source: RGD
  • neuronal cell body Source: RGD
  • synaptic vesicle Source: RGD
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi192 – 1921H → A: Abolishes decarboxylase activity. 2 Publications
Mutagenesisi192 – 1921H → Q: Reduces decarboxylase activity by 96%. 2 Publications
Mutagenesisi252 – 2521D → A or E: Abolishes decarboxylase activity. 1 Publication
Mutagenesisi271 – 2711D → A: Abolishes decarboxylase activity. 2 Publications
Mutagenesisi271 – 2711D → E: Reduces decarboxylase activity by 65%. 2 Publications
Mutagenesisi296 – 2961S → A: Abolishes decarboxylase activity. 1 Publication
Mutagenesisi300 – 3001N → A: Reduces decarboxylase activity by 75%. 1 Publication
Mutagenesisi302 – 3021H → Q: Reduces decarboxylase activity by 99.8%. 1 Publication
Mutagenesisi303 – 3031K → A or R: Abolishes decarboxylase activity. 1 Publication
Mutagenesisi332 – 3321Y → A or F: Abolishes decarboxylase activity. 1 Publication
Mutagenesisi355 – 3551R → A: Abolishes decarboxylase activity. 1 Publication
Mutagenesisi355 – 3551R → K: No effect. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 480480Aromatic-L-amino-acid decarboxylasePRO_0000146942Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei303 – 3031N6-(pyridoxal phosphate)lysine

Proteomic databases

PaxDbiP14173.
PRIDEiP14173.

PTM databases

PhosphoSiteiP14173.

Expressioni

Gene expression databases

ExpressionAtlasiP14173. baseline and differential.
GenevestigatoriP14173.

Interactioni

Subunit structurei

Homodimer.

Structurei

3D structure databases

ProteinModelPortaliP14173.
SMRiP14173. Positions 1-475.
ModBaseiSearch...
MobiDBiSearch...

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

eggNOGiCOG0076.
GeneTreeiENSGT00760000119205.
HOVERGENiHBG000944.
InParanoidiP14173.
KOiK01593.
OMAiCSFDKLL.
OrthoDBiEOG75B851.
PhylomeDBiP14173.
TreeFamiTF313863.

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.

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_006251475.2.
XP_008768474.1. XM_008770252.1.
UniGeneiRn.11064.

Genome annotation databases

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

Cross-referencesi

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_006251475.2.
XP_008768474.1. XM_008770252.1.
UniGeneiRn.11064.

3D structure databases

ProteinModelPortaliP14173.
SMRiP14173. Positions 1-475.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiP14173.

Proteomic databases

PaxDbiP14173.
PRIDEiP14173.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi1644.
RGDi2494. Ddc.

Phylogenomic databases

eggNOGiCOG0076.
GeneTreeiENSGT00760000119205.
HOVERGENiHBG000944.
InParanoidiP14173.
KOiK01593.
OMAiCSFDKLL.
OrthoDBiEOG75B851.
PhylomeDBiP14173.
TreeFamiTF313863.

Enzyme and pathway databases

UniPathwayiUPA00747; UER00734.
BioCyciMetaCyc:MONOMER-15070.
ReactomeiREACT_295841. Catecholamine biosynthesis.
REACT_336165. Serotonin and melatonin biosynthesis.

Miscellaneous databases

NextBioi602949.
PROiP14173.

Gene expression databases

ExpressionAtlasiP14173. baseline and differential.
GenevestigatoriP14173.

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

« Hide 'large scale' publications
  1. "Molecular cloning and sequencing of a cDNA of rat dopa decarboxylase: partial amino acid homologies with other enzymes synthesizing catecholamines."
    Tanaka T., Horio Y., Taketoshi M., Imamura I., Ando-Yamamoto M., Kangawa K., Matsuo H., Kurodo M., Wada H.
    Proc. Natl. Acad. Sci. U.S.A. 86:8142-8146(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  3. "Distinct promoters direct neuronal and nonneuronal expression of rat aromatic L-amino acid decarboxylase."
    Albert V.R., Lee M.R., Bolden A.H., Wurzburger R.J., Aguanno A.
    Proc. Natl. Acad. Sci. U.S.A. 89:12053-12057(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-67.
    Strain: Sprague-Dawley.
  4. "Functionally important residues of aromatic L-amino acid decarboxylase probed by sequence alignment and site-directed mutagenesis."
    Ishii S., Mizugichi H., Nishino J., Hayashi H., Kagamiyama H.
    J. Biochem. 120:369-376(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF HIS-192; ASP-252; ASP-271; SER-296; LYS-303; TYR-332 AND ARG-355, COFACTOR.
  5. "Mutation of residues in the coenzyme binding pocket of Dopa decarboxylase. Effects on catalytic properties."
    Bertoldi M., Castellani S., Bori Voltattorni C.
    Eur. J. Biochem. 268:2975-2981(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF HIS-192; ASP-271; ASN-300 AND HIS-302.

Entry informationi

Entry nameiDDC_RAT
AccessioniPrimary (citable) accession number: P14173
Secondary accession number(s): Q6LEG4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: May 27, 2015
This is version 127 of the entry and version 1 of the sequence. [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

External Data

Dasty 3

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 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.