ID O44285_9NEOP Unreviewed; 350 AA.
AC O44285;
DT 01-JUN-1998, integrated into UniProtKB/TrEMBL.
DT 01-JUN-1998, sequence version 1.
DT 24-JAN-2024, entry version 82.
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 Rothschildia forbesi.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Saturniidae; Saturniinae; Attacini; Rothschildia.
OX NCBI_TaxID=63988 {ECO:0000313|EMBL:AAC47886.1};
RN [1] {ECO:0000313|EMBL:AAC47886.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=9479702; DOI=10.1006/mpev.1997.9999;
RA Friedlander T.P., Horst K.R., Regier J.C., Mitter C., Peigler R.S.,
RA Fang Q.Q.;
RT "Two nuclear genes yield concordant relationships within Attacini
RT (Lepidoptera: Saturniidae).";
RL Mol. Phylogenet. Evol. 9:131-140(1998).
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 -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|ARBA:ARBA00009533, ECO:0000256|RuleBase:RU000382}.
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DR EMBL; AF015060; AAC47886.1; -; mRNA.
DR AlphaFoldDB; O44285; -.
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 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:SF167; 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 Catecholamine biosynthesis {ECO:0000256|ARBA:ARBA00022584};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR602129-50}.
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:AAC47886.1"
FT NON_TER 350
FT /evidence="ECO:0000313|EMBL:AAC47886.1"
SQ SEQUENCE 350 AA; 39727 MW; A8EF17E9DAA886F8 CRC64;
SSPACTELEV VMMDWLGQML ALPDEFLAKS GGEGGGVIQG TASEATLVAL LGAKARITQR
IKEQHPEWTD YEILSKLVGY ANKQAHSSVE RAGLLGGIKF RSLQPGSDRR LNGEILREAM
DEDIRNGLIP FYVVATLGTT SSCVFDDLDG IGDICKARDI WLHVDAAYAG SAFICPEYRY
LMKGIEKADS FNFNPHKWLL VNFDCSAMWL KQPRWIVDAF NVDPLYLKHD QQGSAPDYRH
WQIPLGRRFR ALKLWFVLRL YGVENLQKHI RKQIALAHLF EKLCNSDERF EIFEEVTMGL
VCFRLKGGNE INEELLRRIN GRGKIHLVPS KIDDVYFLRL AICSRMSEES
//