ID L7QR14_9NEOP Unreviewed; 427 AA.
AC L7QR14;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 28.
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 Coronidia orithea.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Geometroidea;
OC Sematuridae; Coronidia.
OX NCBI_TaxID=753290 {ECO:0000313|EMBL:AGB87575.1};
RN [1] {ECO:0000313|EMBL:AGB87575.1}
RP NUCLEOTIDE SEQUENCE.
RA Regier J.C., Mitter C., Solis M.A., Hayden J.E., Landry B., Nuss M.,
RA Simonsen T.J., Yen S.-H., Zwick A., Cummings M.P.;
RT "A molecular phylogeny for the pyraloid moths (Lepidoptera: Pyraloidea) and
RT its implications for higher-level classification.";
RL Syst. Entomol. 37:635-656(2012).
RN [2] {ECO:0000313|EMBL:AGB87575.1}
RP NUCLEOTIDE SEQUENCE.
RG LepTree.net;
RA Regier J.C.;
RT "Assembling the Tree of Life Lepidoptera.";
RL Submitted (MAR-2012) 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; JQ785765; AGB87575.1; -; mRNA.
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; 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 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 274
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AGB87575.1"
FT NON_TER 427
FT /evidence="ECO:0000313|EMBL:AGB87575.1"
SQ SEQUENCE 427 AA; 48046 MW; FD642AC3D3F9D7CC CRC64;
VPSVKPGYLR PLVPEQAPQQ AEPWTAVMAD IERVVMSGVT HWHSPRFHAY FPTANSYPAI
VADMLSGAIA CIGFTWIASP ACTELEVVML DWLGQMLGLP EEFLARSGGE AGGVIQGTAS
EATLVALLGA KARAMQSIKE QHPDWTETQI LSKLVGYCNK QAHSSVERAG LLGGXKLRPL
QTPSRRLHGN ELREAMEEDI RNGLIPFYVV ATLGTTSSCT FDALDEIGDV CAEYENVWLH
VDAAYAGSSF ICPEYRYLMK GIEKADSFNF NPHKWLLVNF DCSAMWLKQP RWIVDAFNVD
PLYLKHDQQG SAPDYRHWQI PLGRRFRALK LWFVLRLYGV ENLQKXIRKX IALAHLFESX
CXADXRFEIX EEVTMGLVCF RLKXSNDLNK ELLRRINGRG KIHXVPSEID GVYFLRXAIC
SRFTEDS
//
