ID D2WJ25_PAPGL Unreviewed; 427 AA.
AC D2WJ25;
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:ACT87710.1};
OS Papilio glaucus (Eastern tiger swallowtail butterfly) (Pterourus glaucus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Papilionidae; Papilioninae; Papilio; Pterourus.
OX NCBI_TaxID=45779 {ECO:0000313|EMBL:ACT87710.1};
RN [1] {ECO:0000313|EMBL:ACT87710.1}
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}.
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DR EMBL; GQ283644; ACT87710.1; -; mRNA.
DR AlphaFoldDB; D2WJ25; -.
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:ACT87710.1"
FT NON_TER 427
FT /evidence="ECO:0000313|EMBL:ACT87710.1"
SQ SEQUENCE 427 AA; 48151 MW; 30FB51D2B8526CF4 CRC64;
VPSVKPGYLR PLVPEQAPDK AEPWTAVMAD IERVVMSGVT HWHSPRFHAY FPTANSYPAI
VADMLSGAIA CIGFTWIASP ACTELEVVML DWLGQMLGLP EVFLARSGGE AGGVIQGTAS
EATLVALLGA KARTMQRVKE QHPEWTDTEI LSKLVGYCNK QAHSSVERAG LLGGVKMRSL
KPDNKHRLRG DTLREAIDED IKNGLIPFYV VATLGTTSSC TFDALDEIGD VCADRDVWLH
VDAAYAGSAF ICPEYRYLMK GVEKADSFNF NPHKWMLVNF DCSAMWLKQP RWIVDAFNVD
PLYLKHDQQG SAPDYRHWQI PLGRRFRALK LWFVLRLYGV ENLQKHIRKH IALAHLFEKM
CTSDERFEIV EEVTMGLVCF RLKGNNDINE DLLRRINGRG KIHLVPSKID DVYFLRLAIC
SRFSEES
//
