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P14173 (DDC_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aromatic-L-amino-acid decarboxylase

Short name=AADC
EC=4.1.1.28
Alternative name(s):
DOPA decarboxylase
Short name=DDC
Gene names
Name:Ddc
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length480 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine (DOPA) to dopamine, L-5-hydroxytryptophan to serotonin and L-tryptophan to tryptamine.

Catalytic activity

L-dopa = dopamine + CO2.

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

Cofactor

Pyridoxal phosphate. Ref.4

Pathway

Catecholamine biosynthesis; dopamine biosynthesis; dopamine from L-tyrosine: step 2/2.

Subunit structure

Homodimer.

Sequence similarities

Belongs to the group II decarboxylase family.

Ontologies

Keywords
   Biological processCatecholamine biosynthesis
   DomainRepeat
   LigandPyridoxal phosphate
   Molecular functionDecarboxylase
Lyase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcatecholamine biosynthetic process

Traceable author statement PubMed 12047348. Source: RGD

cellular amino acid metabolic process

Inferred from electronic annotation. Source: InterPro

cellular response to alkaloid

Inferred from expression pattern PubMed 18696327. Source: RGD

cellular response to drug

Inferred from expression pattern PubMed 18602388. Source: RGD

cellular response to growth factor stimulus

Inferred from expression pattern PubMed 17306206. Source: RGD

circadian rhythm

Inferred from expression pattern PubMed 12047348. Source: RGD

dopamine biosynthetic process

Inferred from direct assay PubMed 12703659. Source: RGD

dopamine metabolic process

Traceable author statement PubMed 7567987. Source: RGD

isoquinoline alkaloid metabolic process

Inferred from expression pattern PubMed 18305432. Source: RGD

multicellular organismal aging

Inferred from expression pattern PubMed 17112516. Source: RGD

phytoalexin metabolic process

Inferred from expression pattern PubMed 19185027. Source: RGD

response to pyrethroid

Inferred from expression pattern PubMed 19017407. Source: RGD

serotonin biosynthetic process

Inferred from direct assay PubMed 10027744. Source: RGD

synaptic vesicle amine transport

Inferred from direct assay PubMed 19903816. Source: RGD

   Cellular_componentaxon

Inferred from direct assay PubMed 19589383. Source: RGD

cytoplasm

Inferred from direct assay PubMed 3379830. Source: RGD

intracellular

Traceable author statement PubMed 7567987. Source: RGD

neuronal cell body

Inferred from direct assay PubMed 19589383. Source: RGD

synaptic vesicle

Inferred from direct assay PubMed 19903816. Source: RGD

   Molecular_functionamino acid binding

Inferred from direct assay PubMed 10569946. Source: RGD

aromatic-L-amino-acid decarboxylase activity

Inferred from direct assay PubMed 10569946PubMed 12047348PubMed 12703659PubMed 3379830. Source: RGD

protein binding

Inferred from physical interaction PubMed 16981894PubMed 19903816. Source: RGD

protein domain specific binding

Inferred from physical interaction PubMed 19903816. Source: RGD

pyridoxal phosphate binding

Inferred from direct assay PubMed 8422386. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 480480Aromatic-L-amino-acid decarboxylase
PRO_0000146942

Regions

Repeat58 – 115581
Repeat118 – 178612
Region58 – 1781212 X approximate tandem repeats

Sites

Binding site821Substrate By similarity
Binding site1481PLP; via amide nitrogen By similarity
Binding site1491PLP By similarity
Binding site1921Substrate By similarity
Binding site2461PLP; via carbonyl oxygen By similarity
Binding site3001PLP By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue3031N6-(pyridoxal phosphate)lysine

Experimental info

Mutagenesis1921H → A: Abolishes decarboxylase activity. Ref.4 Ref.5
Mutagenesis1921H → Q: Reduces decarboxylase activity by 96%. Ref.4 Ref.5
Mutagenesis2521D → A or E: Abolishes decarboxylase activity. Ref.4
Mutagenesis2711D → A: Abolishes decarboxylase activity. Ref.4 Ref.5
Mutagenesis2711D → E: Reduces decarboxylase activity by 65%. Ref.4 Ref.5
Mutagenesis2961S → A: Abolishes decarboxylase activity. Ref.4
Mutagenesis3001N → A: Reduces decarboxylase activity by 75%. Ref.5
Mutagenesis3021H → Q: Reduces decarboxylase activity by 99.8%. Ref.5
Mutagenesis3031K → A or R: Abolishes decarboxylase activity. Ref.4
Mutagenesis3321Y → A or F: Abolishes decarboxylase activity. Ref.4
Mutagenesis3551R → A: Abolishes decarboxylase activity. Ref.4
Mutagenesis3551R → K: No effect. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P14173 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: 1E1D077488704574

FASTA48054,053
        10         20         30         40         50         60 
MDSREFRRRG KEMVDYIADY LDGIEGRPVY PDVEPGYLRA LIPTTAPQEP ETYEDIIRDI 

        70         80         90        100        110        120 
EKIIMPGVTH WHSPYFFAYF PTASSYPAML ADMLCGAIGC IGFSWAASPA CTELETVMMD 

       130        140        150        160        170        180 
WLGKMLELPE AFLAGRAGEG GGVIQGSASE ATLVALLAAR TKMIRQLQAA SPELTQAALM 

       190        200        210        220        230        240 
EKLVAYTSDQ AHSSVERAGL IGGVKIKAIP SDGNYSMRAA ALREALERDK AAGLIPFFVV 

       250        260        270        280        290        300 
VTLGTTSCCS FDNLLEVGPI CNQEGVWLHI DAAYAGSAFI CPEFRYLLNG VEFADSFNFN 

       310        320        330        340        350        360 
PHKWLLVNFD CSAMWVKKRT DLTEAFNMDP VYLRHSHQDS GLITDYRHWQ IPLGRRFRSL 

       370        380        390        400        410        420 
KMWFVFRMYG VKGLQAYIRK HVKLSHEFES LVRQDPRFEI CTEVILGLVC FRLKGSNQLN 

       430        440        450        460        470        480 
ETLLQRINSA KKIHLVPCRL RDKFVLRFAV CSRTVESAHV QLAWEHIRDL ASSVLRAEKE 

« Hide

References

« Hide 'large scale' references
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L33001 expand/collapse EMBL AC list , 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.
PIRDCRTA. A33994.
RefSeqNP_001257781.1. NM_001270852.1.
NP_001257782.1. NM_001270853.1.
NP_036677.1. NM_012545.4.
XP_006251537.1. XM_006251475.1.
UniGeneRn.11064.

3D structure databases

ProteinModelPortalP14173.
SMRP14173. Positions 1-475.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteP14173.

Proteomic databases

PaxDbP14173.
PRIDEP14173.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000005851; ENSRNOP00000005851; ENSRNOG00000004327.
ENSRNOT00000073892; ENSRNOP00000064520; ENSRNOG00000004327.
GeneID24311.
KEGGrno:24311.
UCSCRGD:2494. rat.

Organism-specific databases

CTD1644.
RGD2494. Ddc.

Phylogenomic databases

eggNOGCOG0076.
GeneTreeENSGT00730000110825.
HOVERGENHBG000944.
KOK01593.
OMAPICNKED.
OrthoDBEOG75B851.
PhylomeDBP14173.
TreeFamTF313863.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-15070.
UniPathwayUPA00747; UER00734.

Gene expression databases

GenevestigatorP14173.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProIPR010977. 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]
PfamPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
PRINTSPR00800. YHDCRBOXLASE.
SUPFAMSSF53383. SSF53383. 1 hit.
PROSITEPS00392. DDC_GAD_HDC_YDC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio602949.
PROP14173.

Entry information

Entry nameDDC_RAT
AccessionPrimary (citable) accession number: P14173
Secondary accession number(s): Q6LEG4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: July 9, 2014
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways