ID   A0A091RRF6_NESNO        Unreviewed;       485 AA.
AC   A0A091RRF6;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 26.
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};
DE   Flags: Fragment;
GN   ORFNames=N333_04022 {ECO:0000313|EMBL:KFQ45210.1};
OS   Nestor notabilis (Kea).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Nestor.
OX   NCBI_TaxID=176057 {ECO:0000313|EMBL:KFQ45210.1, ECO:0000313|Proteomes:UP000053840};
RN   [1] {ECO:0000313|EMBL:KFQ45210.1, ECO:0000313|Proteomes:UP000053840}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N333 {ECO:0000313|EMBL:KFQ45210.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; KK931320; KFQ45210.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091RRF6; -.
DR   Proteomes; UP000053840; 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   CDD; cd06450; DOPA_deC_like; 1.
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); 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   PANTHER; PTHR11999:SF70; AROMATIC-L-AMINO-ACID DECARBOXYLASE; 1.
DR   PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
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:UP000053840}.
FT   MOD_RES         303
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
FT   NON_TER         485
FT                   /evidence="ECO:0000313|EMBL:KFQ45210.1"
SQ   SEQUENCE   485 AA;  54862 MW;  6A27E77C33E7C54D CRC64;
     MDAAEFRKRG KEMVDYIADY LEKIDERQVF PDVEPGYLRP LIADCAPQNP ETFEDVFKDI
     EKIIMPGVTH WHSPYFFAYF PAASSFPALL ADMLCGGIGC VGFSWAASPA CTELETVMLD
     WLGKMINLPE EFLAGKDGHG GGVIQGSASE ATLISLLAAR TKTIRRVQSE KPELTEADIM
     GRLVAYASDQ AHSSVERAAL IGGVKIKNVS SDDTFSVCGS ALKKVLDEDK ASGLIPFFFC
     ATLGTTPCCS FDKLLELGPI CNKENIWMHI DAAYAGSAFI CPEFRHLLNG VEFADSFNFN
     PHKWLLVNFD CSAMWVKKRS DLTGAFKLEP LYLQHHHQES GLVTDYRHWQ IPLGRRFRSL
     KLWFVLRMYG VTGLQEHIRK HVRLSHQFEH LVRQDERFEI CAEVILGLVC FRLKGSNELN
     EALLKSINAA KKIHLVPCHL REKFVLRFAI CSRTVESTHI KFAWQHISQL ATDLLKTWEQ
     NHHQQ
//