ID D2WJ15_9NEOP Unreviewed; 427 AA.
AC D2WJ15;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 38.
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:ACT87700.1};
OS Macrotheca sp. JCR-2009.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Pyraloidea;
OC Pyralidae; Galleriinae; Macrotheca.
OX NCBI_TaxID=655172 {ECO:0000313|EMBL:ACT87700.1};
RN [1] {ECO:0000313|EMBL:ACT87700.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=19954545; DOI=10.1186/1471-2148-9-280;
RA Regier J.C., Zwick A., Cummings M.P., Kawahara A.Y., Cho S., Weller S.,
RA Roe A., Baixeras J., Brown J.W., Parr C., Davis D.R., Epstein M.,
RA Hallwachs W., Hausmann A., Janzen D.H., Kitching I.J., Solis M.A.,
RA Yen S.H., Bazinet A.L., Mitter C.;
RT "Toward reconstructing the evolution of advanced moths and butterflies
RT (Lepidoptera: Ditrysia): an initial molecular study.";
RL BMC Evol. Biol. 9:280-280(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 -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|ARBA:ARBA00009533, ECO:0000256|RuleBase:RU000382}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GQ283634; ACT87700.1; -; mRNA.
DR AlphaFoldDB; D2WJ15; -.
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:ACT87700.1"
FT NON_TER 427
FT /evidence="ECO:0000313|EMBL:ACT87700.1"
SQ SEQUENCE 427 AA; 48219 MW; A39FCF9465E1D465 CRC64;
VPSVKPGYLR PLVPEQAPQQ PEPWTAVMAD IERVVMSGVT HWHSPRFHAY FPTANSYPAI
VADMLSGAIA CIGFTWIASP ACTELEVVML DWLGQMLGLP NEFLARSNGE AGGVIQGTAS
EATLVALLGA KARTMQRVKS LHPEWTETEI LSKLVGYCNK QAHSSVERAG LLGGVTLRSL
KPDSKRRLRG DILRDAMEED IRKGLIPFYV VATLGTTSSC TFDVLDEIGD VCNSHEVWLH
VDAAYAGSAF ICPEYRYLMK GIEKADSFNF NPHKWLLVNF DCSALWLKQP RWIIDAFNVD
PLYLKHDQQG SAPDYRHWQI PLGRRFRALK LWFVLRLYGV ENLQKHIRKH IAFAHLFENL
CTSDTRFELF EEVTMGLVCF RLKGSNELNK ELLKRINGRG KIHLVPSEID GVYFLRLAIC
SRFTEES
//
