ID O44274_ANTPE Unreviewed; 434 AA.
AC O44274;
DT 01-JUN-1998, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 2.
DT 27-MAR-2024, entry version 85.
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 Antheraea pernyi (Chinese oak silk moth) (Bombyx pernyi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Saturniidae; Saturniinae; Saturniini; Antheraea.
OX NCBI_TaxID=7119 {ECO:0000313|EMBL:AAC47875.2};
RN [1] {ECO:0000313|EMBL:AAC47875.2}
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).
RN [2] {ECO:0000313|EMBL:AAC47875.2}
RP NUCLEOTIDE SEQUENCE.
RA Regier J.C.;
RL Submitted (MAY-2003) 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; AF015049; AAC47875.2; -; mRNA.
DR AlphaFoldDB; O44274; -.
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 281
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAC47875.2"
FT NON_TER 434
FT /evidence="ECO:0000313|EMBL:AAC47875.2"
SQ SEQUENCE 434 AA; 49059 MW; 5A98EC91C162EEFC CRC64;
NIRDRQVVPS VKPGYLRPLV PDQAPEQAEP WTAVMADIER VVMSGVTHWQ SPKFHAYFPT
ASSYPGIVAD MLCGAIACIG FTWIASPACT ELEVVMLDWL GQMLALPEEF LAKSGGEGGG
VIQGTASEAT LVALLGAKAR ITQRVKEQHP EWTDYEILSK LVGYANKQAH SSVERAGLLG
GVKLRALQPG KDRRLNGEIL REAMDEDIRN GLIPFYVVAT LGTTSSCVFD DLESIGDICK
SRDIWLHVDA AYAGSAFICP EYRYLMKGIE KTDSFNFNPH KWLLVNFDCS AMWLKQPRWI
VDAFNVDPLY LKHDQQGSAP DYRHWQIPLG RRFRALKLWF VLRLYGVENL QKHIRKQIAL
AHLFEKLCSS DERFEIFEEV TMGLVCFRLK GNNEINEELL RRINGRGKIH LVPSKIDDVY
FLRLAICSRM SEES
//
