DDC_BOVIN
ID DDC_BOVIN Reviewed; 487 AA.
AC P27718; Q0V8S3;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, 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:0000250|UniProtKB:P80041};
DE AltName: Full=DOPA decarboxylase;
DE Short=DDC;
GN Name=DDC;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2166204; DOI=10.1016/0169-328x(90)90013-4;
RA Kang U., Joh T.H.;
RT "Deduced amino acid sequence of bovine aromatic L-amino acid decarboxylase:
RT homology to other decarboxylases.";
RL Brain Res. Mol. Brain Res. 8:83-87(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
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; M74029; AAC41615.1; -; mRNA.
DR EMBL; BT026145; ABG66984.1; -; mRNA.
DR PIR; A43758; A43758.
DR RefSeq; NP_776332.1; NM_173907.2.
DR RefSeq; XP_010802269.1; XM_010803967.1.
DR AlphaFoldDB; P27718; -.
DR SMR; P27718; -.
DR STRING; 9913.ENSBTAP00000051814; -.
DR PaxDb; P27718; -.
DR PRIDE; P27718; -.
DR GeneID; 280762; -.
DR KEGG; bta:280762; -.
DR CTD; 1644; -.
DR eggNOG; KOG0628; Eukaryota.
DR InParanoid; P27718; -.
DR OrthoDB; 856958at2759; -.
DR UniPathway; UPA00747; UER00734.
DR Proteomes; UP000009136; 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 2: Evidence at transcript level;
KW Acetylation; Catecholamine biosynthesis; Decarboxylase; Lyase;
KW Pyridoxal phosphate; Reference proteome; Repeat.
FT CHAIN 1..487
FT /note="Aromatic-L-amino-acid decarboxylase"
FT /id="PRO_0000146937"
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"
FT CONFLICT 170..171
FT /note="AS -> RA (in Ref. 1; AAC41615)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="M -> T (in Ref. 1; AAC41615)"
FT /evidence="ECO:0000305"
FT CONFLICT 221..225
FT /note="ALQEA -> RCRR (in Ref. 1; AAC41615)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="F -> SC (in Ref. 1; AAC41615)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="E -> K (in Ref. 1; AAC41615)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 487 AA; 54294 MW; 8F104C610A332FFD CRC64;
MNASEFRRRG KEMVDYVADY LEGIEGRQVF PDVDPGYLRP LIPTTAPQEP ETFEAIIEDI
EKIIMPGVTH WHSPYFFAYF PTASSYPAML ADMLCGAIGC IGFSWAASPA CTELETVMMD
WLGKMLQLPE AFLAGEAGEG GGVIQGTASE ATLVALLAAR TKVTRHLQAA SPELMQAAIM
EKLVAYASDQ AHSSVEKAGL IGGVRLKAIP SDGKFAMRAS ALQEALERDK AAGLIPFFVV
ATLGTTSCCS FDNLLEVGPI CHEEGLWLHV DAAYAGSAFI CPEFRHLLNG VEFADSFNFN
PHKWLLVNFD CSAMWVKKRT DLTGAFRLDP VYLRHSHQDS GLITDYRHWQ LPLGRRFRSL
KMWFVFRMYG VKGLQAYIRK HVQLSHAFEA LVRQDTRFEI CAEVILGLVC FRLKGSNKLN
EALLESINSA KKIHLVPCSL RDRFVLRFAI CSRTVELAHV QLAWEHIQEM AATVLRAQGE
EKAEIKN
