P22781 (DDC_CAVPO) Reviewed, UniProtKB/Swiss-Prot

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

Cavia porcellus (Guinea pig) [Reference proteome]

Taxonomic identifier

10141 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Hystricognathi › Caviidae › Cavia

Protein attributes

Sequence length	480 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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.
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 dopamine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	aromatic-L-amino-acid decarboxylase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
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_0000146938
Regions
	Repeat	58 – 115	58	1
	Repeat	118 – 178	61	2
	Region	58 – 178	121	2 X approximate tandem repeats
Sites
	Binding site	82	1	Substrate By similarity
	Binding site	192	1	Substrate By similarity
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine By similarity
	Modified residue	303	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P22781 [UniParc]. Last modified August 1, 1991. Version 1. Checksum: 46AB0649DB20F5A4	FASTA	480	54,151
	10 20 30 40 50 60 MNASEFRRRG KEMVDYVANY LEGIESRLVY PDVEPGYLRP LIPSSAPEEP ETYEDIIGDI 70 80 90 100 110 120 ERIIMPGVTH WNSPYFFAYF PTANSYPSML ADMLCGAISC IGFSWAASPA CTELETVMLD 130 140 150 160 170 180 WLGKMLRLPD AFLAGNAGMG GGVIQGSASE ATLVALLAAR TKVIRRLQAA SPELTQAAIM 190 200 210 220 230 240 EKLVAYASDQ AHSSVERAGL IGGVRMKLIP SDSNFAMRAS ALREALERDK AAGLIPFFVV 250 260 270 280 290 300 ATLGTTNCCS FDSLLEVGPI CNQEEMWLHI DAAYAGSAFI CPEFRHLLDG VEFADSFNFN 310 320 330 340 350 360 PHKWLLVNFD CSAMWVKQRT DLIGAFKLDP VYLKHGHQDS GLITDYRHWQ IPLGRRFRSL 370 380 390 400 410 420 KMWFVFRMYG IKGLQAHIRK HVQLAHEFES LVRQDPRFEI CMEVTLGLVC FRLKGSNQLN 430 440 450 460 470 480 ETLLKRINSA RKIHLVPCHL RDKFVLRFRI CSRQVESDHV QQAWQHIRQL ASSVLRLERA

References

[1]	"Molecular cloning of guinea-pig aromatic-L-amino acid decarboxylase cDNA." Taketoshi M., Horio Y., Imamura I., Tanaka T., Fukui H., Wada H. Biochem. Biophys. Res. Commun. 170:1229-1235(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	M58049 mRNA. Translation: AAA51530.1.
PIR	DEGPA. A35710.
RefSeq	NP_001166414.1. NM_001172943.1.
3D structure databases
ProteinModelPortal	P22781.
SMR	P22781. Positions 1-475.
ModBase	Search...
Protein-protein interaction databases
STRING	10141.ENSCPOP00000004824.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	100135516.
Organism-specific databases
CTD	1644.
Phylogenomic databases
eggNOG	COG0076.
HOGENOM	HOG000121941.
HOVERGEN	HBG000944.
Enzyme and pathway databases
UniPathway	UPA00747; UER00734.
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...

Entry information

Entry name

DDC_CAVPO

Accession

Primary (citable) accession number: P22781

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	August 1, 1991
Last modified:	April 3, 2013
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program