ID B9U719_9NEOP Unreviewed; 350 AA.
AC B9U719;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 43.
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:ACD01554.1};
OS Acosmeryx naga.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Sphingidae; Macroglossinae; Macroglossini; Acosmeryx.
OX NCBI_TaxID=522778 {ECO:0000313|EMBL:ACD01554.1};
RN [1] {ECO:0000313|EMBL:ACD01554.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AToL-Lep-ID AYK-04-2570 {ECO:0000313|EMBL:ACD01554.1};
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; EU479124; ACD01554.1; -; mRNA.
DR AlphaFoldDB; B9U719; -.
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; 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 197
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACD01554.1"
FT NON_TER 350
FT /evidence="ECO:0000313|EMBL:ACD01554.1"
SQ SEQUENCE 350 AA; 39816 MW; DFB79E5E2E70627A CRC64;
ASPACTELEV VMLDWLGQML GLPEEFLARS GGEAGGVIQG TASEATLVAL LGAKSRMMQK
LKEEHPEWSE TDILGKLVGY CNKQAHSSVE RAGLLGGVKL RSLQPDSKRR LRGDILREAM
DEDISKGLIP FYVVATLGTT SSCTFDALDE IGDVCNSRNI WLHVDAAYAG SAFICPEYRY
LMKGVEKADS FNFNPHKWML VNFDCSAMWL KQPRWIVDAF NVDPLYLKHD QQGSAPDYRH
WQIPLGRRFR SLKLWFVLRL YGVENLQKHI RKQIALAHLF EKLLTEDERF ELFEEVTMGL
VCFRLKGSNE INEELLRRIN GRGKIHLVPS KIDDVYFLRL AICSRFTEDS
//