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Database: UniProt
Entry: B9U769_HIPCE
LinkDB: B9U769_HIPCE
Original site: B9U769_HIPCE 
ID   B9U769_HIPCE            Unreviewed;       427 AA.
AC   B9U769;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 45.
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   Name=DDC {ECO:0000313|EMBL:ACD01604.1};
OS   Hippotion celerio (Grapevine hawk moth) (Sphinx tisiphone).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Sphingidae; Macroglossinae; Macroglossini; Hippotion.
OX   NCBI_TaxID=283870 {ECO:0000313|EMBL:ACD01604.1};
RN   [1] {ECO:0000313|EMBL:ACD01604.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AToL-Lep-ID IJK-02-5932 {ECO:0000313|EMBL:ACD01604.1};
RX   PubMed=19492095; DOI=10.1371/journal.pone.0005719;
RA   Kawahara A.Y., Mignault A.A., Regier J.C., Kitching I.J., Mitter C.;
RT   "Phylogeny and biogeography of hawkmoths (Lepidoptera: Sphingidae):
RT   evidence from five nuclear genes.";
RL   PLoS ONE 4:e5719-e5719(2009).
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   -!- 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; EU479174; ACD01604.1; -; mRNA.
DR   AlphaFoldDB; B9U769; -.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
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:SF167; 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   2: Evidence at transcript level;
KW   Catecholamine biosynthesis {ECO:0000256|ARBA:ARBA00022584};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR602129-50}.
FT   MOD_RES         274
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACD01604.1"
FT   NON_TER         427
FT                   /evidence="ECO:0000313|EMBL:ACD01604.1"
SQ   SEQUENCE   427 AA;  48324 MW;  48205F4DBC5E67DA CRC64;
     VPSVKPGYLR PLVPEQAPKE AEPWTAVMAD IERVVMSGVT HWQSPRFHAY FPTANSYPAI
     VADMLSGAIA CIGFTWIASP ACTELEVVML DWLGQMLGLP EQFLARSGGE GGGVIQGTAS
     EATLVALLGA KSRTMQKLKE EHPEWTDTEI LGKLVGYCNK QAHSSVERAG LLGGVKLRSL
     QPDDKRRLRG DILRKAMDED ISKGLIPFYV VATLGTTSSC TFDALDEIGD VCNERDIWLH
     VDAAYAGSAF ICPEYRHFMK GIEKADSFNF NPHKWMLVNF DCSAMWLKQP RWIVDAFNVD
     PLYLKHDQQG SAPDYRHWQI PLGRRFRSLK LWFVLRLYGV ENLQKHIRKQ IALAHLFEKH
     LGSDERFELF EEVTMGLVCF RLKGSNEINE ELLRRINGRG KIHLVPSKID DVYFLRLAIC
     SRFTDDR
//
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