ID Q9BNZ0_HYLLI Unreviewed; 350 AA.
AC Q9BNZ0;
DT 01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2001, sequence version 1.
DT 27-MAR-2024, entry version 83.
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;
OS Hyles lineata (White-lined sphinx moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Sphingidae; Macroglossinae; Macroglossini; Hyles.
OX NCBI_TaxID=103890 {ECO:0000313|EMBL:AAK08686.1};
RN [1] {ECO:0000313|EMBL:AAK08686.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=11476639; DOI=10.1006/mpev.2001.0963;
RA Regier J.C., Mitter C., Friedlander T.P., Peigler R.S.;
RT "Re: Phylogenetic relationships in Sphingidae (Insecta: Lepidoptera):
RT initial evidence from two nuclear genes.";
RL Mol. Phylogenet. Evol. 20:311-316(2001).
RN [2] {ECO:0000313|EMBL:ABW39088.1}
RP NUCLEOTIDE SEQUENCE.
RA Regier J.C.;
RT "PCR primers that amplify across Panarthropoda.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|ARBA:ARBA00009533, ECO:0000256|RuleBase:RU000382}.
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DR EMBL; AF234589; AAK08686.1; -; mRNA.
DR EMBL; EU032821; ABW39088.1; -; mRNA.
DR AlphaFoldDB; Q9BNZ0; -.
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 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; 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 2: Evidence at transcript level;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382}.
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:AAK08686.1"
FT NON_TER 350
FT /evidence="ECO:0000313|EMBL:AAK08686.1"
SQ SEQUENCE 350 AA; 39722 MW; 6492C3C4DA311D0F CRC64;
ASPACTELEV VMLDWLGQML GLPEQFLARS GGEGGGVIQG TASEATLVAL LGAKSRTMQK
LKEEHPEWSD TDILGKLVGY CNKQAHSSVE RAGLLGGVKL RSLQPDSKRR LRGDILREAM
DEDISKGLIP FYVVATLGTT SSCTFDALDE IGDVCNERDV WLHVDAAYAG SAFICPEYRH
FMKGIEKADS FNFNPHKWML VNFDCSAMWL KQPRWIVDAF NVDPLYLKHD QQGSAPDYRH
WQIPLGRRFR SLKLWFVLRL YGVENLQKHI RKQIALAHLF EKLLASDERF ELFEEVTMGL
VCFRLKGSNE INEELLRRIN GRGKIHLVPS KIDDVYFLRL AICSRFTDDS
//
