DDC_CAEEL
ID DDC_CAEEL Reviewed; 905 AA.
AC P34751; Q23619;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 3.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Probable aromatic-L-amino-acid decarboxylase;
DE Short=AADC;
DE EC=4.1.1.28;
DE AltName: Full=DOPA decarboxylase;
DE Short=DDC;
GN Name=hdl-1; Synonyms=aad-1; ORFNames=ZK829.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 281-905.
RC STRAIN=Bristol N2;
RX PubMed=8382340; DOI=10.1007/bf00277125;
RA Marra M.A., Prasad S.S., Baillie D.L.;
RT "Molecular analysis of two genes between let-653 and let-56 in the unc-
RT 22(IV) region of Caenorhabditis elegans.";
RL Mol. Gen. Genet. 236:289-298(1993).
CC -!- FUNCTION: Catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine
CC (DOPA) to dopamine, L-5-hydroxytryptophan to serotonin and L-tryptophan
CC to tryptamine.
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 -!- 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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- PATHWAY: Catecholamine biosynthesis; dopamine biosynthesis; dopamine
CC from L-tyrosine: step 2/2.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000305}.
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DR EMBL; Z73899; CAA98072.2; -; Genomic_DNA.
DR EMBL; Z11576; CAA77663.1; -; mRNA.
DR PIR; T28020; T28020.
DR RefSeq; NP_502265.2; NM_069864.4.
DR AlphaFoldDB; P34751; -.
DR SMR; P34751; -.
DR STRING; 6239.ZK829.2; -.
DR PaxDb; P34751; -.
DR PRIDE; P34751; -.
DR EnsemblMetazoa; ZK829.2.1; ZK829.2.1; WBGene00001839.
DR GeneID; 178129; -.
DR KEGG; cel:CELE_ZK829.2; -.
DR UCSC; ZK829.2; c. elegans.
DR CTD; 178129; -.
DR WormBase; ZK829.2; CE40593; WBGene00001839; hdl-1.
DR eggNOG; KOG0628; Eukaryota.
DR HOGENOM; CLU_014028_0_0_1; -.
DR InParanoid; P34751; -.
DR OMA; KGVACWF; -.
DR OrthoDB; 856958at2759; -.
DR PhylomeDB; P34751; -.
DR UniPathway; UPA00747; UER00734.
DR PRO; PR:P34751; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00001839; Expressed in adult organism and 1 other tissue.
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: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: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 Pfam; PF00282; Pyridoxal_deC; 1.
DR PRINTS; PR00800; YHDCRBOXLASE.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 2: Evidence at transcript level;
KW Catecholamine biosynthesis; Decarboxylase; Lyase; Pyridoxal phosphate;
KW Reference proteome.
FT CHAIN 1..905
FT /note="Probable aromatic-L-amino-acid decarboxylase"
FT /id="PRO_0000146943"
FT REGION 250..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 861..905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 492
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 591
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT MOD_RES 648
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 415..422
FT /note="HPNFHSFY -> SSKFSFIL (in Ref. 2; CAA77663)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 905 AA; 102004 MW; 47F6151DBB422CB0 CRC64;
MSEKGETLIE DTAEIEFEQT VDKTQQWGRL KNAAAFSLFR DLHMNESLQR KHARSDYKVY
DLNNRVIFHV INTTAMPITK DGPFCLKVMN KDKKSVAKFL RNEPKRSYKQ TGLASLFGCC
SDTEDTMEVL DDNGLIIATS FLHHDQFRGI LITMKDPAGK VLIGIQASRD QKDVFAVSGP
DNRYLGEIRQ KIISSGNSTD NYKGVACWFS TEVSLNVKVF FMAAAFLIEI DYFSETKSRQ
APFRTPEADY LNPIIKTPPH NERVPKMKTN ISKTRKKKGK VSDASKDSRP SETKKETLMM
PEIHHTKHFD SIGGEEQAFA KKEKVEEFKP TEAVKEEVDV NGMSRDQFRN AAKKVVDYLM
KQDESIRAAR CSPALKPGYL KALLPPKAPQ KAEDIDDILE DYHKLIVPGL SHSSHPNFHS
FYPAGNSFHC LLADLLGGHI GDAGFYWTSN PALTELEVLM MDWLGEMMAL PKEFLLFPEA
SRGGGCMQRS DTESNFLVLV AARTDMIRRM KQRDKRLRSS DILARLVAYT SSDARRSIKM
KMAAEVAMVK MRVLPTDQNF ILRGDTLHAA IMADIERGLI PFFVGANFGT SGPCSFDHLH
ELGPVCREHG TWLHVDAAYA GTALICPEIR GLMRGIDWAD SFCTTPSKLI IAVCDVCCLW
VRDRHKLQHA SLENHPDLPF KGLPTSQRVG ALKIWFMIRS FGVENLQNQI REHIRLGQVM
TKILQKDLRF EVCNKVVMGL ICFRAKSNDM FNKALLYRCN ETGNVSLASC VLQNKFVIRM
CINSPKCSEE DLDSAYKLIC NEYDILKPFQ YRIEVMNQAE LETFIRDPAK IHSSAEVSRR
FPVVNPLEPC RSLAQISSQM HTAEYADPPG KSNKSPQVAA KGELPSAAPP SSRTPNSDIS
EKSDR
