Aromatic-L-amino-acid decarboxylase - Rattus norvegicus (Rat)

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P14173 (DDC_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 110. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	480 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Catecholamine biosynthesis
Domain	Repeat
Ligand	Pyridoxal phosphate
Molecular function	Decarboxylase Lyase
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	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 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_component	axon Inferred from direct assay PubMed 19589383. Source: RGD neuronal cell body Inferred from direct assay PubMed 19589383. Source: RGD synaptic vesicle Inferred from direct assay PubMed 19903816. Source: RGD
Molecular_function	amino acid binding Inferred from direct assay PubMed 10569946. Source: RGD aromatic-L-amino-acid decarboxylase activity Inferred from direct assay PubMed 10569946 PubMed 12047348 PubMed 12703659 PubMed 3379830. Source: RGD pyridoxal phosphate binding Inferred from direct assay PubMed 8422386. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 480

480

Aromatic-L-amino-acid decarboxylase

PRO_0000146942

Regions

Repeat

58 – 115

Repeat

118 – 178

Region

58 – 178

121

2 X approximate tandem repeats

Sites

Binding site

Substrate By similarity

Binding site

192

Substrate By similarity

Amino acid modifications

Modified residue

N-acetylmethionine By similarity

Modified residue

303

N6-(pyridoxal phosphate)lysine

Experimental info

Mutagenesis

192

H → A: Abolishes decarboxylase activity. Ref.4 Ref.5

Mutagenesis

192

H → Q: Reduces decarboxylase activity by 96%. Ref.4 Ref.5

Mutagenesis

252

D → A or E: Abolishes decarboxylase activity. Ref.4

Mutagenesis

271

D → A: Abolishes decarboxylase activity. Ref.4 Ref.5

Mutagenesis

271

D → E: Reduces decarboxylase activity by 65%. Ref.4 Ref.5

Mutagenesis

296

S → A: Abolishes decarboxylase activity. Ref.4

Mutagenesis

300

N → A: Reduces decarboxylase activity by 75%. Ref.5

Mutagenesis

302

H → Q: Reduces decarboxylase activity by 99.8%. Ref.5

Mutagenesis

303

K → A or R: Abolishes decarboxylase activity. Ref.4

Mutagenesis

332

Y → A or F: Abolishes decarboxylase activity. Ref.4

Mutagenesis

355

R → A: Abolishes decarboxylase activity. Ref.4

Mutagenesis

355

R → K: No effect. Ref.4

Sequences

Sequence

Length

Mass (Da)

Tools

P14173 [UniParc].

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

FASTA

480

54,053

        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' referencesShow '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 L33000 Genomic DNA. Translation: AAA40646.1. M27716 mRNA. Translation: AAA41087.1. BC087032 mRNA. Translation: AAH87032.1. L03417 Genomic DNA. Translation: AAA99905.1.
IPI	IPI00470246.
PIR	DCRTA. A33994.
RefSeq	NP_001257781.1. NM_001270852.1. NP_001257782.1. NM_001270853.1. NP_036677.1. NM_012545.4.
UniGene	Rn.11064.
3D structure databases
ProteinModelPortal	P14173.
SMR	P14173. Positions 1-475.
ModBase	Search...
PTM databases
PhosphoSite	P14173.
Proteomic databases
PaxDb	P14173.
PRIDE	P14173.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000005851; ENSRNOP00000005851; ENSRNOG00000004327. ENSRNOT00000073892; ENSRNOP00000064520; ENSRNOG00000004327.
GeneID	24311.
KEGG	rno:24311.
UCSC	RGD:2494. rat.
Organism-specific databases
CTD	1644.
RGD	2494. Ddc.
Phylogenomic databases
eggNOG	COG0076.
GeneTree	ENSGT00550000074275.
HOVERGEN	HBG000944.
KO	K01593.
OrthoDB	EOG4B8JCZ.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-15070.
UniPathway	UPA00747; UER00734.
Gene expression databases
ArrayExpress	P14173.
Genevestigator	P14173.
GermOnline	ENSRNOG00000004327. Rattus norvegicus.
Family and domain databases
Gene3D	3.40.640.10. 1 hit. 3.90.1150.10. 1 hit.
InterPro	IPR010977. 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]
Pfam	PF00282. Pyridoxal_deC. 1 hit. [Graphical view]
PRINTS	PR00800. YHDCRBOXLASE.
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
PROSITE	PS00392. DDC_GAD_HDC_YDC. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	602949.

Entry information

Entry name

DDC_RAT

Accession

Primary (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:	April 3, 2013
This is version 110 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents