DDC_PIG
ID DDC_PIG Reviewed; 486 AA.
AC P80041;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Aromatic-L-amino-acid decarboxylase;
DE Short=AADC;
DE EC=4.1.1.28 {ECO:0000269|PubMed:8670114};
DE AltName: Full=DOPA decarboxylase {ECO:0000303|PubMed:8670114};
DE Short=DDC {ECO:0000303|PubMed:8670114};
GN Name=DDC;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=8670114; DOI=10.1042/bj3150249;
RA Moore P.S., Dominici P., Borri-Voltattorni C.;
RT "Cloning and expression of pig kidney dopa decarboxylase: comparison of the
RT naturally occurring and recombinant enzymes.";
RL Biochem. J. 315:249-256(1996).
RN [2]
RP PROTEIN SEQUENCE OF 1-485, AND ACETYLATION AT MET-1.
RC TISSUE=Kidney;
RX PubMed=1935935; DOI=10.1111/j.1432-1033.1991.tb16295.x;
RA Maras B., Dominici P., Barra D., Bossa F., Borri-Voltattorni C.;
RT "Pig kidney 3,4-dihydroxyphenylalanine (dopa) decarboxylase. Primary
RT structure and relationships to other amino acid decarboxylases.";
RL Eur. J. Biochem. 201:385-391(1991).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE
RP AND CARBIDOPA, COFACTOR, AND SUBUNIT.
RX PubMed=11685243; DOI=10.1038/nsb1101-963;
RA Burkhard P., Dominici P., Borri-Voltattorni C., Jansonius J.N.,
RA Malashkevich V.N.;
RT "Structural insight into Parkinson's disease treatment from drug-inhibited
RT DOPA decarboxylase.";
RL Nat. Struct. Biol. 8:963-967(2001).
CC -!- FUNCTION: Catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine
CC (DOPA) to dopamine and L-5-hydroxytryptophan to serotonin.
CC {ECO:0000269|PubMed:8670114}.
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:0000269|PubMed:8670114};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12273;
CC Evidence={ECO:0000269|PubMed:8670114};
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:0000269|PubMed:8670114};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18534;
CC Evidence={ECO:0000269|PubMed:8670114};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:11685243};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=200 uM for L-dopa {ECO:0000269|PubMed:8670114};
CC Vmax=5959 nmol/min/mg enzyme {ECO:0000269|PubMed:8670114};
CC -!- PATHWAY: Catecholamine biosynthesis; dopamine biosynthesis; dopamine
CC from L-tyrosine: step 2/2. {ECO:0000269|PubMed:8670114}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11685243}.
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000305}.
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DR EMBL; S82290; AAB47157.1; -; mRNA.
DR PIR; S17848; S17848.
DR RefSeq; NP_999019.1; NM_213854.1.
DR PDB; 1JS3; X-ray; 2.25 A; A/B=1-486.
DR PDB; 1JS6; X-ray; 2.60 A; A/B=1-486.
DR PDBsum; 1JS3; -.
DR PDBsum; 1JS6; -.
DR AlphaFoldDB; P80041; -.
DR SMR; P80041; -.
DR STRING; 9823.ENSSSCP00000019955; -.
DR BindingDB; P80041; -.
DR ChEMBL; CHEMBL2841; -.
DR iPTMnet; P80041; -.
DR PaxDb; P80041; -.
DR PeptideAtlas; P80041; -.
DR GeneID; 396857; -.
DR CTD; 1644; -.
DR eggNOG; KOG0628; Eukaryota.
DR InParanoid; P80041; -.
DR BioCyc; MetaCyc:MON-14992; -.
DR BRENDA; 4.1.1.28; 6170.
DR SABIO-RK; P80041; -.
DR UniPathway; UPA00747; UER00734.
DR EvolutionaryTrace; P80041; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0036467; F:5-hydroxy-L-tryptophan decarboxylase activity; IEA:RHEA.
DR GO; GO:0004058; F:aromatic-L-amino-acid decarboxylase activity; IBA:GO_Central.
DR GO; GO:0016831; F:carboxy-lyase activity; IBA:GO_Central.
DR GO; GO:0036468; F:L-dopa decarboxylase activity; IEA:RHEA.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
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:0042416; P:dopamine biosynthetic process; IEA:UniProtKB-UniPathway.
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; Catecholamine biosynthesis; Decarboxylase;
KW Direct protein sequencing; Lyase; Pyridoxal phosphate; Reference proteome;
KW Repeat.
FT CHAIN 1..486
FT /note="Aromatic-L-amino-acid decarboxylase"
FT /id="PRO_0000146941"
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:0000269|PubMed:11685243,
FT ECO:0007744|PDB:1JS3"
FT BINDING 148
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P20711"
FT BINDING 149
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P20711"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11685243,
FT ECO:0007744|PDB:1JS3"
FT BINDING 246
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P20711"
FT BINDING 300
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P20711"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:1935935"
FT MOD_RES 303
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|PubMed:11685243"
FT HELIX 3..22
FT /evidence="ECO:0007829|PDB:1JS3"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:1JS3"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:1JS3"
FT HELIX 53..62
FT /evidence="ECO:0007829|PDB:1JS3"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:1JS3"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:1JS3"
FT HELIX 86..98
FT /evidence="ECO:0007829|PDB:1JS3"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:1JS3"
FT HELIX 109..125
FT /evidence="ECO:0007829|PDB:1JS3"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:1JS3"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:1JS3"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:1JS3"
FT HELIX 148..170
FT /evidence="ECO:0007829|PDB:1JS3"
FT HELIX 176..182
FT /evidence="ECO:0007829|PDB:1JS3"
FT STRAND 183..188
FT /evidence="ECO:0007829|PDB:1JS3"
FT HELIX 193..202
FT /evidence="ECO:0007829|PDB:1JS3"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:1JS3"
FT HELIX 219..231
FT /evidence="ECO:0007829|PDB:1JS3"
FT STRAND 235..244
FT /evidence="ECO:0007829|PDB:1JS3"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:1JS3"
FT HELIX 254..263
FT /evidence="ECO:0007829|PDB:1JS3"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:1JS3"
FT HELIX 275..280
FT /evidence="ECO:0007829|PDB:1JS3"
FT TURN 282..284
FT /evidence="ECO:0007829|PDB:1JS3"
FT HELIX 285..288
FT /evidence="ECO:0007829|PDB:1JS3"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:1JS3"
FT STRAND 295..299
FT /evidence="ECO:0007829|PDB:1JS3"
FT HELIX 301..304
FT /evidence="ECO:0007829|PDB:1JS3"
FT STRAND 312..317
FT /evidence="ECO:0007829|PDB:1JS3"
FT HELIX 319..323
FT /evidence="ECO:0007829|PDB:1JS3"
FT HELIX 324..326
FT /evidence="ECO:0007829|PDB:1JS3"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:1JS3"
FT STRAND 349..351
FT /evidence="ECO:0007829|PDB:1JS3"
FT HELIX 359..394
FT /evidence="ECO:0007829|PDB:1JS3"
FT STRAND 398..400
FT /evidence="ECO:0007829|PDB:1JS3"
FT STRAND 406..415
FT /evidence="ECO:0007829|PDB:1JS3"
FT HELIX 417..430
FT /evidence="ECO:0007829|PDB:1JS3"
FT STRAND 432..434
FT /evidence="ECO:0007829|PDB:1JS6"
FT STRAND 436..440
FT /evidence="ECO:0007829|PDB:1JS3"
FT STRAND 443..449
FT /evidence="ECO:0007829|PDB:1JS3"
FT HELIX 457..475
FT /evidence="ECO:0007829|PDB:1JS3"
SQ SEQUENCE 486 AA; 53936 MW; 6CE5978531A9FFA4 CRC64;
MNASDFRRRG KEMVDYMADY LEGIEGRQVY PDVQPGYLRP LIPATAPQEP DTFEDILQDV
EKIIMPGVTH WHSPYFFAYF PTASSYPAML ADMLCGAIGC IGFSWAASPA CTELETVMMD
WLGKMLQLPE AFLAGEAGEG GGVIQGSASE ATLVALLAAR TKVVRRLQAA SPGLTQGAVL
EKLVAYASDQ AHSSVERAGL IGGVKLKAIP SDGKFAMRAS ALQEALERDK AAGLIPFFVV
ATLGTTSCCS FDNLLEVGPI CHEEDIWLHV DAAYAGSAFI CPEFRHLLNG VEFADSFNFN
PHKWLLVNFD CSAMWVKRRT DLTGAFKLDP VYLKHSHQGS GLITDYRHWQ LPLGRRFRSL
KMWFVFRMYG VKGLQAYIRK HVQLSHEFEA FVLQDPRFEV CAEVTLGLVC FRLKGSDGLN
EALLERINSA RKIHLVPCRL RGQFVLRFAI CSRKVESGHV RLAWEHIRGL AAELLAAEEG
KAEIKS
