DDC_HUMAN
ID DDC_HUMAN Reviewed; 480 AA.
AC P20711; C9IYA0; E7ER62; E7EU95; Q16723; Q5W5T9; Q75MJ6;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Aromatic-L-amino-acid decarboxylase {ECO:0000303|PubMed:2590185};
DE Short=AADC {ECO:0000303|PubMed:2590185};
DE EC=4.1.1.28;
DE AltName: Full=DOPA decarboxylase {ECO:0000303|PubMed:1612608};
DE Short=DDC {ECO:0000303|PubMed:1612608};
GN Name=DDC {ECO:0000303|PubMed:15532536, ECO:0000312|HGNC:HGNC:2719};
GN Synonyms=AADC {ECO:0000303|PubMed:2590185};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT VAL-17.
RC TISSUE=Pheochromocytoma;
RX PubMed=2590185; DOI=10.1016/0006-291x(89)91772-5;
RA Ichinose H., Kurosawa Y., Titani K., Fujita K., Nagatsu T.;
RT "Isolation and characterization of a cDNA clone encoding human aromatic L-
RT amino acid decarboxylase.";
RL Biochem. Biophys. Res. Commun. 164:1024-1030(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT VAL-17.
RX PubMed=1612608; DOI=10.1016/0888-7543(92)90275-w;
RA Scherer L.J., McPherson J.D., Wasmuth J.J., Marsh L.J.;
RT "Human dopa decarboxylase: localization to human chromosome 7p11 and
RT characterization of hepatic cDNAs.";
RL Genomics 13:469-471(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISEASE, AND VARIANT VAL-17.
RX PubMed=1540578; DOI=10.1021/bi00123a004;
RA Sumi-Ichinose C., Ichinose H., Takahashi E., Hori T., Nagatsu T.;
RT "Molecular cloning of genomic DNA and chromosomal assignment of the gene
RT for human aromatic L-amino acid decarboxylase, the enzyme for catecholamine
RT and serotonin biosynthesis.";
RL Biochemistry 31:2229-2238(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING, TISSUE
RP SPECIFICITY, AND VARIANT VAL-17.
RC TISSUE=Placenta;
RX PubMed=15532536; DOI=10.1023/b:nere.0000042207.05071.ea;
RA Vassilacopoulou D.S., Sideris D.C., Vassiliou A.G., Fragoulis E.G.;
RT "Identification and characterization of a novel form of the human L-dopa
RT decarboxylase mRNA.";
RL Neurochem. Res. 29:1817-1823(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-17; ASP-61; LEU-210;
RP VAL-217; LEU-239; ILE-239 AND GLN-462.
RG NIEHS SNPs program;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-17.
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-67, AND VARIANT VAL-17.
RX PubMed=8510497; DOI=10.1016/0169-328x(93)90006-b;
RA Van Thai A., Coste E., Allen J.M., Palmiter R.D., Weber M.J.;
RT "Identification of a neuron-specific promoter of human aromatic L-amino
RT acid decarboxylase gene.";
RL Brain Res. Mol. Brain Res. 17:227-238(1993).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 68-105.
RX PubMed=1395716; DOI=10.1159/000133384;
RA Craig S.P., Thai A.L., Weber M., Craig I.W.;
RT "Localisation of the gene for human aromatic L-amino acid decarboxylase
RT (DDC) to chromosome 7p13-->p11 by in situ hybridisation.";
RL Cytogenet. Cell Genet. 61:114-116(1992).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), COFACTOR-BINDING SITES, AND SUBUNIT.
RX PubMed=22143761; DOI=10.1073/pnas.1111456108;
RA Giardina G., Montioli R., Gianni S., Cellini B., Paiardini A.,
RA Voltattorni C.B., Cutruzzola F.;
RT "Open conformation of human DOPA decarboxylase reveals the mechanism of PLP
RT addition to Group II decarboxylases.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20514-20519(2011).
RN [12]
RP VARIANTS AADCD VAL-91; SER-102; ARG-147; PHE-250; THR-275 AND LEU-309.
RA Chang Y.T., Mues G., McPherson J.D., Bedell J., Marsh J.L., Hyland K.,
RA Courtwright K.H., Summers J.W.;
RT "Mutations in the human aromatic L-amino acid decarboxylase gene.";
RL J. Inherit. Metab. Dis. 21:4-4(1998).
RN [13]
RP VARIANTS VAL-17; LEU-210 AND VAL-217.
RX PubMed=10391209; DOI=10.1038/10290;
RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA Lander E.S.;
RT "Characterization of single-nucleotide polymorphisms in coding regions of
RT human genes.";
RL Nat. Genet. 22:231-238(1999).
RN [14]
RP ERRATUM OF PUBMED:10391209.
RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA Lander E.S.;
RL Nat. Genet. 23:373-373(1999).
RN [15]
RP VARIANT AADCD SER-102.
RX PubMed=14991824; DOI=10.1002/ana.20055;
RA Chang Y.T., Sharma R., Marsh J.L., McPherson J.D., Bedell J.A., Knust A.,
RA Braeutigam C., Hoffmann G.F., Hyland K.;
RT "Levodopa-responsive aromatic L-amino acid decarboxylase deficiency.";
RL Ann. Neurol. 55:435-438(2004).
RN [16]
RP VARIANTS AADCD HIS-47; PHE-250; GLN-347 AND ILE-408.
RX PubMed=15079002; DOI=10.1212/wnl.62.7.1058;
RA Pons R., Ford B., Chiriboga C.A., Clayton P.T., Hinton V., Hyland K.,
RA Sharma R., De Vivo D.C.;
RT "Aromatic L-amino acid decarboxylase deficiency: clinical features,
RT treatment, and prognosis.";
RL Neurology 62:1058-1065(2004).
CC -!- FUNCTION: Catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine
CC (DOPA) to dopamine and L-5-hydroxytryptophan to serotonin.
CC {ECO:0000250|UniProtKB:P80041}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-dopa = CO2 + dopamine; Xref=Rhea:RHEA:12272,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57504,
CC ChEBI:CHEBI:59905; EC=4.1.1.28;
CC Evidence={ECO:0000250|UniProtKB:P80041};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-hydroxy-L-tryptophan + H(+) = CO2 + serotonin;
CC Xref=Rhea:RHEA:18533, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:58266, ChEBI:CHEBI:350546; EC=4.1.1.28;
CC Evidence={ECO:0000250|UniProtKB:P80041};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:22143761};
CC -!- PATHWAY: Catecholamine biosynthesis; dopamine biosynthesis; dopamine
CC from L-tyrosine: step 2/2. {ECO:0000250|UniProtKB:P80041}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:22143761}.
CC -!- INTERACTION:
CC P20711; P10275: AR; NbExp=2; IntAct=EBI-1632155, EBI-608057;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P20711-1; Sequence=Displayed;
CC Name=2; Synonyms=alt-DDC {ECO:0000303|PubMed:15532536};
CC IsoId=P20711-2; Sequence=VSP_046569, VSP_046570;
CC Name=3;
CC IsoId=P20711-3; Sequence=VSP_047175;
CC Name=4;
CC IsoId=P20711-4; Sequence=VSP_047176;
CC -!- TISSUE SPECIFICITY: [Isoform 2]: High expression in kidney.
CC {ECO:0000269|PubMed:15532536}.
CC -!- DISEASE: Aromatic L-amino-acid decarboxylase deficiency (AADCD)
CC [MIM:608643]: An inborn error in neurotransmitter metabolism that leads
CC to combined serotonin and catecholamine deficiency. It causes
CC developmental and psychomotor delay, poor feeding, lethargy, ptosis,
CC intermittent hypothermia, gastrointestinal disturbances. The onset is
CC early in infancy and inheritance is autosomal recessive.
CC {ECO:0000269|PubMed:14991824, ECO:0000269|PubMed:15079002,
CC ECO:0000269|Ref.12}. Note=The disease is caused by variants affecting
CC the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/ddc/";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Aromatic L-amino-acid decarboxylase
CC entry;
CC URL="https://en.wikipedia.org/wiki/Aromatic-L-amino-acid_decarboxylase";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/DDCID50590ch7p12.html";
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DR EMBL; M76180; AAA58437.1; -; mRNA.
DR EMBL; M88700; AAA20894.1; -; mRNA.
DR EMBL; M84592; AAD40482.1; -; Genomic_DNA.
DR EMBL; M84600; AAD40482.1; JOINED; Genomic_DNA.
DR EMBL; M84593; AAD40482.1; JOINED; Genomic_DNA.
DR EMBL; M84594; AAD40482.1; JOINED; Genomic_DNA.
DR EMBL; M84596; AAD40482.1; JOINED; Genomic_DNA.
DR EMBL; M84597; AAD40482.1; JOINED; Genomic_DNA.
DR EMBL; M84595; AAD40482.1; JOINED; Genomic_DNA.
DR EMBL; M84598; AAD40482.1; JOINED; Genomic_DNA.
DR EMBL; M84599; AAD40482.1; JOINED; Genomic_DNA.
DR EMBL; M84588; AAD40482.1; JOINED; Genomic_DNA.
DR EMBL; M84589; AAD40482.1; JOINED; Genomic_DNA.
DR EMBL; M84590; AAD40482.1; JOINED; Genomic_DNA.
DR EMBL; M84591; AAD40482.1; JOINED; Genomic_DNA.
DR EMBL; AJ310724; CAC84071.1; -; mRNA.
DR EMBL; AY526322; AAS00092.1; -; Genomic_DNA.
DR EMBL; AC018705; AAS01995.1; -; Genomic_DNA.
DR EMBL; BC000485; AAH00485.1; -; mRNA.
DR EMBL; BC008366; AAH08366.1; -; mRNA.
DR EMBL; AH005280; AAB59432.1; -; Genomic_DNA.
DR EMBL; S46516; AAB23675.1; -; Genomic_DNA.
DR CCDS; CCDS5511.1; -. [P20711-1]
DR CCDS; CCDS56485.1; -. [P20711-3]
DR CCDS; CCDS56486.1; -. [P20711-4]
DR CCDS; CCDS56487.1; -. [P20711-2]
DR PIR; A33663; DCHUA.
DR RefSeq; NP_000781.1; NM_000790.3. [P20711-1]
DR RefSeq; NP_001076440.1; NM_001082971.1. [P20711-1]
DR RefSeq; NP_001229815.1; NM_001242886.1.
DR RefSeq; NP_001229816.1; NM_001242887.1.
DR RefSeq; NP_001229817.1; NM_001242888.1. [P20711-3]
DR RefSeq; NP_001229818.1; NM_001242889.1. [P20711-4]
DR RefSeq; NP_001229819.1; NM_001242890.1. [P20711-2]
DR PDB; 3RBF; X-ray; 2.90 A; A/B=1-480.
DR PDB; 3RBL; X-ray; 3.24 A; A/B=1-480.
DR PDB; 3RCH; X-ray; 2.80 A; A/B=1-480.
DR PDBsum; 3RBF; -.
DR PDBsum; 3RBL; -.
DR PDBsum; 3RCH; -.
DR AlphaFoldDB; P20711; -.
DR SMR; P20711; -.
DR BioGRID; 108011; 3.
DR DIP; DIP-40563N; -.
DR IntAct; P20711; 4.
DR STRING; 9606.ENSP00000403644; -.
DR BindingDB; P20711; -.
DR ChEMBL; CHEMBL1843; -.
DR DrugBank; DB00915; Amantadine.
DR DrugBank; DB12783; Benserazide.
DR DrugBank; DB00190; Carbidopa.
DR DrugBank; DB00260; Cycloserine.
DR DrugBank; DB06262; Droxidopa.
DR DrugBank; DB13848; Fluorodopa (18F).
DR DrugBank; DB00875; Flupentixol.
DR DrugBank; DB01235; Levodopa.
DR DrugBank; DB00968; Methyldopa.
DR DrugBank; DB00114; Pyridoxal phosphate.
DR DrugBank; DB00150; Tryptophan.
DR DrugCentral; P20711; -.
DR PhosphoSitePlus; P20711; -.
DR BioMuta; DDC; -.
DR DMDM; 311033369; -.
DR jPOST; P20711; -.
DR MassIVE; P20711; -.
DR MaxQB; P20711; -.
DR PaxDb; P20711; -.
DR PeptideAtlas; P20711; -.
DR PRIDE; P20711; -.
DR ProteomicsDB; 17724; -.
DR ProteomicsDB; 18381; -.
DR ProteomicsDB; 53778; -. [P20711-1]
DR ProteomicsDB; 7633; -.
DR Antibodypedia; 2793; 529 antibodies from 47 providers.
DR DNASU; 1644; -.
DR Ensembl; ENST00000357936.9; ENSP00000350616.5; ENSG00000132437.18. [P20711-1]
DR Ensembl; ENST00000380984.4; ENSP00000370371.4; ENSG00000132437.18. [P20711-2]
DR Ensembl; ENST00000426377.5; ENSP00000395069.1; ENSG00000132437.18. [P20711-3]
DR Ensembl; ENST00000431062.5; ENSP00000399184.1; ENSG00000132437.18. [P20711-4]
DR Ensembl; ENST00000444124.7; ENSP00000403644.2; ENSG00000132437.18. [P20711-1]
DR Ensembl; ENST00000615193.4; ENSP00000484104.1; ENSG00000132437.18. [P20711-4]
DR GeneID; 1644; -.
DR KEGG; hsa:1644; -.
DR MANE-Select; ENST00000444124.7; ENSP00000403644.2; NM_001082971.2; NP_001076440.2.
DR UCSC; uc003tpf.5; human. [P20711-1]
DR CTD; 1644; -.
DR DisGeNET; 1644; -.
DR GeneCards; DDC; -.
DR HGNC; HGNC:2719; DDC.
DR HPA; ENSG00000132437; Group enriched (intestine, kidney, retina).
DR MalaCards; DDC; -.
DR MIM; 107930; gene.
DR MIM; 608643; phenotype.
DR neXtProt; NX_P20711; -.
DR OpenTargets; ENSG00000132437; -.
DR Orphanet; 35708; Aromatic L-amino acid decarboxylase deficiency.
DR PharmGKB; PA140; -.
DR VEuPathDB; HostDB:ENSG00000132437; -.
DR eggNOG; KOG0628; Eukaryota.
DR GeneTree; ENSGT00940000156004; -.
DR HOGENOM; CLU_011856_3_0_1; -.
DR InParanoid; P20711; -.
DR OMA; NPGFNWS; -.
DR OrthoDB; 856958at2759; -.
DR PhylomeDB; P20711; -.
DR TreeFam; TF313863; -.
DR BioCyc; MetaCyc:HS05635-MON; -.
DR BRENDA; 4.1.1.28; 2681.
DR PathwayCommons; P20711; -.
DR Reactome; R-HSA-209905; Catecholamine biosynthesis.
DR Reactome; R-HSA-209931; Serotonin and melatonin biosynthesis.
DR SABIO-RK; P20711; -.
DR SignaLink; P20711; -.
DR SIGNOR; P20711; -.
DR UniPathway; UPA00747; UER00734.
DR BioGRID-ORCS; 1644; 9 hits in 1070 CRISPR screens.
DR ChiTaRS; DDC; human.
DR GenomeRNAi; 1644; -.
DR Pharos; P20711; Tclin.
DR PRO; PR:P20711; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P20711; protein.
DR Bgee; ENSG00000132437; Expressed in jejunal mucosa and 125 other tissues.
DR ExpressionAtlas; P20711; baseline and differential.
DR Genevisible; P20711; HS.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0008021; C:synaptic vesicle; IEA:Ensembl.
DR GO; GO:0036467; F:5-hydroxy-L-tryptophan decarboxylase activity; IEA:RHEA.
DR GO; GO:0016597; F:amino acid binding; IEA:Ensembl.
DR GO; GO:0004058; F:aromatic-L-amino-acid decarboxylase activity; IDA:UniProtKB.
DR GO; GO:0016831; F:carboxy-lyase activity; IBA:GO_Central.
DR GO; GO:0019899; F:enzyme binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0036468; F:L-dopa decarboxylase activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:Ensembl.
DR GO; GO:0015842; P:aminergic neurotransmitter loading into synaptic vesicle; IEA:Ensembl.
DR GO; GO:0006584; P:catecholamine metabolic process; IBA:GO_Central.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR GO; GO:0071312; P:cellular response to alkaloid; IEA:Ensembl.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IEA:Ensembl.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
DR GO; GO:0042416; P:dopamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0033076; P:isoquinoline alkaloid metabolic process; IEA:Ensembl.
DR GO; GO:0010259; P:multicellular organism aging; IEA:Ensembl.
DR GO; GO:0052314; P:phytoalexin metabolic process; IEA:Ensembl.
DR GO; GO:0046684; P:response to pyrethroid; IEA:Ensembl.
DR GO; GO:0042427; P:serotonin biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR010977; Aromatic_deC.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR021115; Pyridoxal-P_BS.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR PRINTS; PR00800; YHDCRBOXLASE.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing;
KW Catecholamine biosynthesis; Decarboxylase; Disease variant; Lyase;
KW Pyridoxal phosphate; Reference proteome; Repeat.
FT CHAIN 1..480
FT /note="Aromatic-L-amino-acid decarboxylase"
FT /id="PRO_0000146939"
FT REPEAT 58..115
FT /note="1"
FT REPEAT 118..178
FT /note="2"
FT REGION 58..178
FT /note="2 X approximate tandem repeats"
FT BINDING 82
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P80041"
FT BINDING 148
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:22143761,
FT ECO:0007744|PDB:3RCH"
FT BINDING 149
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:22143761,
FT ECO:0007744|PDB:3RCH"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P80041"
FT BINDING 246
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:22143761,
FT ECO:0007744|PDB:3RCH"
FT BINDING 300
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:22143761,
FT ECO:0007744|PDB:3RCH"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P80041"
FT MOD_RES 303
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|PubMed:22143761"
FT VAR_SEQ 68..145
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_047175"
FT VAR_SEQ 146..238
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_047176"
FT VAR_SEQ 316..338
FT /note="VKKRTDLTGAFRLDPTYLKHSHQ -> SRQPVRMLRLKKTCLVSAVVRRS
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15532536"
FT /id="VSP_046569"
FT VAR_SEQ 339..480
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15532536"
FT /id="VSP_046570"
FT VARIANT 17
FT /note="M -> V (in dbSNP:rs6264)"
FT /evidence="ECO:0000269|PubMed:10391209,
FT ECO:0000269|PubMed:1540578, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:15532536, ECO:0000269|PubMed:1612608,
FT ECO:0000269|PubMed:2590185, ECO:0000269|PubMed:8510497,
FT ECO:0000269|Ref.5"
FT /id="VAR_014788"
FT VARIANT 47
FT /note="P -> H (in AADCD; dbSNP:rs780542462)"
FT /evidence="ECO:0000269|PubMed:15079002"
FT /id="VAR_046137"
FT VARIANT 61
FT /note="E -> D (in dbSNP:rs11575292)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_019214"
FT VARIANT 91
FT /note="A -> V (in AADCD; dbSNP:rs137853211)"
FT /evidence="ECO:0000269|Ref.12"
FT /id="VAR_046138"
FT VARIANT 102
FT /note="G -> S (in AADCD; dbSNP:rs137853207)"
FT /evidence="ECO:0000269|PubMed:14991824, ECO:0000269|Ref.12"
FT /id="VAR_019309"
FT VARIANT 147
FT /note="S -> R (in AADCD; dbSNP:rs137853210)"
FT /evidence="ECO:0000269|Ref.12"
FT /id="VAR_046139"
FT VARIANT 210
FT /note="P -> L (in dbSNP:rs6262)"
FT /evidence="ECO:0000269|PubMed:10391209, ECO:0000269|Ref.5"
FT /id="VAR_014789"
FT VARIANT 217
FT /note="M -> V (in dbSNP:rs6263)"
FT /evidence="ECO:0000269|PubMed:10391209, ECO:0000269|Ref.5"
FT /id="VAR_014790"
FT VARIANT 239
FT /note="M -> I (in dbSNP:rs11575377)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_019215"
FT VARIANT 239
FT /note="M -> L (in dbSNP:rs11575376)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_019216"
FT VARIANT 250
FT /note="S -> F (in AADCD; dbSNP:rs137853208)"
FT /evidence="ECO:0000269|PubMed:15079002, ECO:0000269|Ref.12"
FT /id="VAR_046140"
FT VARIANT 275
FT /note="A -> T (in AADCD; dbSNP:rs137853212)"
FT /evidence="ECO:0000269|Ref.12"
FT /id="VAR_046141"
FT VARIANT 309
FT /note="F -> L (in AADCD; dbSNP:rs137853209)"
FT /evidence="ECO:0000269|Ref.12"
FT /id="VAR_046142"
FT VARIANT 347
FT /note="R -> Q (in AADCD; dbSNP:rs201951824)"
FT /evidence="ECO:0000269|PubMed:15079002"
FT /id="VAR_046143"
FT VARIANT 408
FT /note="L -> I (in AADCD)"
FT /evidence="ECO:0000269|PubMed:15079002"
FT /id="VAR_046144"
FT VARIANT 462
FT /note="R -> Q (in dbSNP:rs11575542)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_019217"
FT CONFLICT 49
FT /note="E -> G (in Ref. 8; AAB59432)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="A -> P (in Ref. 3; AAD40482)"
FT /evidence="ECO:0000305"
FT HELIX 3..22
FT /evidence="ECO:0007829|PDB:3RCH"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:3RCH"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:3RCH"
FT HELIX 53..63
FT /evidence="ECO:0007829|PDB:3RCH"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:3RCH"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:3RCH"
FT HELIX 86..98
FT /evidence="ECO:0007829|PDB:3RCH"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:3RBL"
FT HELIX 109..125
FT /evidence="ECO:0007829|PDB:3RCH"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:3RCH"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:3RCH"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:3RCH"
FT HELIX 148..169
FT /evidence="ECO:0007829|PDB:3RCH"
FT HELIX 176..180
FT /evidence="ECO:0007829|PDB:3RCH"
FT STRAND 183..188
FT /evidence="ECO:0007829|PDB:3RCH"
FT HELIX 193..201
FT /evidence="ECO:0007829|PDB:3RCH"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:3RCH"
FT HELIX 219..231
FT /evidence="ECO:0007829|PDB:3RCH"
FT STRAND 235..244
FT /evidence="ECO:0007829|PDB:3RCH"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:3RCH"
FT HELIX 254..263
FT /evidence="ECO:0007829|PDB:3RCH"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:3RCH"
FT HELIX 275..280
FT /evidence="ECO:0007829|PDB:3RCH"
FT TURN 282..284
FT /evidence="ECO:0007829|PDB:3RCH"
FT HELIX 285..288
FT /evidence="ECO:0007829|PDB:3RCH"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:3RCH"
FT STRAND 295..299
FT /evidence="ECO:0007829|PDB:3RCH"
FT HELIX 302..305
FT /evidence="ECO:0007829|PDB:3RCH"
FT STRAND 312..317
FT /evidence="ECO:0007829|PDB:3RCH"
FT HELIX 319..323
FT /evidence="ECO:0007829|PDB:3RCH"
FT HELIX 359..393
FT /evidence="ECO:0007829|PDB:3RCH"
FT STRAND 398..400
FT /evidence="ECO:0007829|PDB:3RCH"
FT STRAND 406..415
FT /evidence="ECO:0007829|PDB:3RCH"
FT HELIX 417..430
FT /evidence="ECO:0007829|PDB:3RCH"
FT STRAND 432..434
FT /evidence="ECO:0007829|PDB:3RCH"
FT STRAND 436..440
FT /evidence="ECO:0007829|PDB:3RCH"
FT STRAND 443..449
FT /evidence="ECO:0007829|PDB:3RCH"
FT HELIX 457..476
FT /evidence="ECO:0007829|PDB:3RCH"
SQ SEQUENCE 480 AA; 53926 MW; 0A2CFF9A39BDE298 CRC64;
MNASEFRRRG KEMVDYMANY MEGIEGRQVY PDVEPGYLRP LIPAAAPQEP DTFEDIINDV
EKIIMPGVTH WHSPYFFAYF PTASSYPAML ADMLCGAIGC IGFSWAASPA CTELETVMMD
WLGKMLELPK AFLNEKAGEG GGVIQGSASE ATLVALLAAR TKVIHRLQAA SPELTQAAIM
EKLVAYSSDQ AHSSVERAGL IGGVKLKAIP SDGNFAMRAS ALQEALERDK AAGLIPFFMV
ATLGTTTCCS FDNLLEVGPI CNKEDIWLHV DAAYAGSAFI CPEFRHLLNG VEFADSFNFN
PHKWLLVNFD CSAMWVKKRT DLTGAFRLDP TYLKHSHQDS GLITDYRHWQ IPLGRRFRSL
KMWFVFRMYG VKGLQAYIRK HVQLSHEFES LVRQDPRFEI CVEVILGLVC FRLKGSNKVN
EALLQRINSA KKIHLVPCHL RDKFVLRFAI CSRTVESAHV QRAWEHIKEL AADVLRAERE
