ID A0A2I0MXK1_COLLI Unreviewed; 440 AA.
AC A0A2I0MXK1;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Aromatic-L-amino-acid decarboxylase {ECO:0000256|ARBA:ARBA00040968};
DE EC=4.1.1.28 {ECO:0000256|ARBA:ARBA00038886};
DE AltName: Full=DOPA decarboxylase {ECO:0000256|ARBA:ARBA00041275};
GN ORFNames=A306_00001718 {ECO:0000313|EMBL:PKK34408.1};
OS Columba livia (Rock dove).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX NCBI_TaxID=8932 {ECO:0000313|EMBL:PKK34408.1, ECO:0000313|Proteomes:UP000053872};
RN [1] {ECO:0000313|EMBL:PKK34408.1, ECO:0000313|Proteomes:UP000053872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Blood {ECO:0000313|EMBL:PKK34408.1};
RX PubMed=23371554; DOI=10.1126/science.1230422;
RA Shapiro M.D., Kronenberg Z., Li C., Domyan E.T., Pan H., Campbell M.,
RA Tan H., Huff C.D., Hu H., Vickrey A.I., Nielsen S.C., Stringham S.A.,
RA Hu H., Willerslev E., Gilbert M.T., Yandell M., Zhang G., Wang J.;
RT "Genomic diversity and evolution of the head crest in the rock pigeon.";
RL Science 339:1063-1067(2013).
CC -!- FUNCTION: Catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine
CC (DOPA) to dopamine and L-5-hydroxytryptophan to serotonin.
CC {ECO:0000256|ARBA:ARBA00037256}.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC -!- PATHWAY: Catecholamine biosynthesis; dopamine biosynthesis; dopamine
CC from L-tyrosine: step 2/2. {ECO:0000256|ARBA:ARBA00037889}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|ARBA:ARBA00009533, ECO:0000256|RuleBase:RU000382}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PKK34408.1}.
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DR EMBL; AKCR02000001; PKK34408.1; -; Genomic_DNA.
DR RefSeq; XP_005507564.1; XM_005507507.1.
DR AlphaFoldDB; A0A2I0MXK1; -.
DR Proteomes; UP000053872; Unassembled WGS sequence.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR GO; GO:0042423; P:catecholamine biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 1.20.1340.10; dopa decarboxylase, N-terminal domain; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 2.
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 PANTHER; PTHR11999:SF70; AROMATIC-L-AMINO-ACID DECARBOXYLASE; 1.
DR PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 1.
DR Pfam; PF00282; Pyridoxal_deC; 2.
DR PRINTS; PR00800; YHDCRBOXLASE.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE 3: Inferred from homology;
KW Catecholamine biosynthesis {ECO:0000256|ARBA:ARBA00022584};
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382};
KW Reference proteome {ECO:0000313|Proteomes:UP000053872}.
FT MOD_RES 255
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 440 AA; 50414 MW; E0BB0310F8F2ED93 CRC64;
MDAAEFRKSG KQMVDYIADY LEKIDKRQVF PDVEPGYLRP LIPDCAPQDP ESFDDVFKDI
EKIIMPGVTH WHSPYFFAYF PSTSSFPALL ADMLCGGIGC VGFSWAASPA CTELETVMMD
WLGKMINLPE EFLAEKGGQG GGVIQGSASE ATLISLLAAR TKTIRRVQSE KPELTEADIM
GRLVAYASDQ FCATLGTTPC CSFDKLFDLG PICNKKSFWM HIDAAYAGSA FICPEFRHLL
NGVEFADSFM FNPHKWLLVN FDCSAMWVKK RSDITSVFKL EPLYLQHQHQ DSGLVTDYRH
WQIPLGRRFR SLKLWFVLRM YGVRGLQEHI RKHIRLSHQF EDLVLQDERF EICAEVVLGL
VCFRLKGSNE LNKELLKSIN EAKKIHLVPC HLREKFVLRF AICSRVVETT HVEFAWQHIS
QLATDLLKAW EQNHHQQHQQ
//
