ID D2WJ32_PIERA Unreviewed; 427 AA.
AC D2WJ32;
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:ACT87717.1};
OS Pieris rapae (Small white butterfly) (Artogeia rapae).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Pieridae; Pierinae; Pieris.
OX NCBI_TaxID=64459 {ECO:0000313|EMBL:ACT87717.1};
RN [1] {ECO:0000313|EMBL:ACT87717.1}
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; GQ283651; ACT87717.1; -; 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:ACT87717.1"
FT NON_TER 427
FT /evidence="ECO:0000313|EMBL:ACT87717.1"
SQ SEQUENCE 427 AA; 48232 MW; 40DF9CFF05262BB1 CRC64;
VPSVKPGYLR PLVPEQAPEK PEPWTAVMAD IERVVMSGVT HWHSPKFHAY FPTANSYPSI
VADMLSGAIA CIGFSWIASP ACTELEVVMM DWLGQMLGLP EEFLARSGGE AGGVIQGTAS
EATLVALLGA KSKAINLTKE QHPEWTXVEI LSKLVGYCNK QAHSSVERAG LLGGVKLRFL
HPDSKRSLRG DTLRDAIKED IQNGLIPFYV VATLGTTSTC AFDALDEIGD VCRENDIWLH
IDAAYAGSSF ICPEYRYLMK GIEKADSFNF NPHKWLLVNF DCSAMWLKQP RWIVDAFNVD
PLYLKYDQQG SAPDYRHWQI PLGRRFRSLK LWFVLRLYGI ENLQKYIRKH IALAHFFEKL
CGEDERFEVV EEVLMGLVCF RLKGDNDLNK ALLRRINGRG KIHLVPSKID DSYFLRFAXC
SRFCEES
//
