DDC_CAVPO
ID DDC_CAVPO Reviewed; 480 AA.
AC P22781;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Aromatic-L-amino-acid decarboxylase;
DE Short=AADC;
DE EC=4.1.1.28 {ECO:0000250|UniProtKB:P80041};
DE AltName: Full=DOPA decarboxylase;
DE Short=DDC;
GN Name=DDC;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2390088; DOI=10.1016/0006-291x(90)90525-r;
RA Taketoshi M., Horio Y., Imamura I., Tanaka T., Fukui H., Wada H.;
RT "Molecular cloning of guinea-pig aromatic-L-amino acid decarboxylase
RT cDNA.";
RL Biochem. Biophys. Res. Commun. 170:1229-1235(1990).
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:0000250|UniProtKB:P20711};
CC -!- PATHWAY: Catecholamine biosynthesis; dopamine biosynthesis; dopamine
CC from L-tyrosine: step 2/2. {ECO:0000250|UniProtKB:P80041}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P20711}.
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000305}.
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DR EMBL; M58049; AAA51530.1; -; mRNA.
DR PIR; A35710; DEGPA.
DR RefSeq; NP_001166414.1; NM_001172943.1.
DR AlphaFoldDB; P22781; -.
DR SMR; P22781; -.
DR STRING; 10141.ENSCPOP00000004824; -.
DR GeneID; 100135516; -.
DR KEGG; cpoc:100135516; -.
DR CTD; 1644; -.
DR eggNOG; KOG0628; Eukaryota.
DR InParanoid; P22781; -.
DR UniPathway; UPA00747; UER00734.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR GO; GO:0036467; F:5-hydroxy-L-tryptophan decarboxylase activity; IEA:RHEA.
DR GO; GO:0036468; F:L-dopa decarboxylase activity; IEA:RHEA.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR GO; GO:0042416; P:dopamine biosynthetic process; IEA:UniProtKB-UniPathway.
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 2: Evidence at transcript level;
KW Acetylation; Catecholamine biosynthesis; Decarboxylase; Lyase;
KW Pyridoxal phosphate; Reference proteome; Repeat.
FT CHAIN 1..480
FT /note="Aromatic-L-amino-acid decarboxylase"
FT /id="PRO_0000146938"
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: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:0000250|UniProtKB:P80041"
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:0000250|UniProtKB:P80041"
FT MOD_RES 303
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P80041"
SQ SEQUENCE 480 AA; 54151 MW; 46AB0649DB20F5A4 CRC64;
MNASEFRRRG KEMVDYVANY LEGIESRLVY PDVEPGYLRP LIPSSAPEEP ETYEDIIGDI
ERIIMPGVTH WNSPYFFAYF PTANSYPSML ADMLCGAISC IGFSWAASPA CTELETVMLD
WLGKMLRLPD AFLAGNAGMG GGVIQGSASE ATLVALLAAR TKVIRRLQAA SPELTQAAIM
EKLVAYASDQ AHSSVERAGL IGGVRMKLIP SDSNFAMRAS ALREALERDK AAGLIPFFVV
ATLGTTNCCS FDSLLEVGPI CNQEEMWLHI DAAYAGSAFI CPEFRHLLDG VEFADSFNFN
PHKWLLVNFD CSAMWVKQRT DLIGAFKLDP VYLKHGHQDS GLITDYRHWQ IPLGRRFRSL
KMWFVFRMYG IKGLQAHIRK HVQLAHEFES LVRQDPRFEI CMEVTLGLVC FRLKGSNQLN
ETLLKRINSA RKIHLVPCHL RDKFVLRFRI CSRQVESDHV QQAWQHIRQL ASSVLRLERA
