ID B9U769_HIPCE Unreviewed; 427 AA.
AC B9U769;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 45.
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:ACD01604.1};
OS Hippotion celerio (Grapevine hawk moth) (Sphinx tisiphone).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Sphingidae; Macroglossinae; Macroglossini; Hippotion.
OX NCBI_TaxID=283870 {ECO:0000313|EMBL:ACD01604.1};
RN [1] {ECO:0000313|EMBL:ACD01604.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AToL-Lep-ID IJK-02-5932 {ECO:0000313|EMBL:ACD01604.1};
RX PubMed=19492095; DOI=10.1371/journal.pone.0005719;
RA Kawahara A.Y., Mignault A.A., Regier J.C., Kitching I.J., Mitter C.;
RT "Phylogeny and biogeography of hawkmoths (Lepidoptera: Sphingidae):
RT evidence from five nuclear genes.";
RL PLoS ONE 4:e5719-e5719(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 -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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; EU479174; ACD01604.1; -; mRNA.
DR AlphaFoldDB; B9U769; -.
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; 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: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 274
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACD01604.1"
FT NON_TER 427
FT /evidence="ECO:0000313|EMBL:ACD01604.1"
SQ SEQUENCE 427 AA; 48324 MW; 48205F4DBC5E67DA CRC64;
VPSVKPGYLR PLVPEQAPKE AEPWTAVMAD IERVVMSGVT HWQSPRFHAY FPTANSYPAI
VADMLSGAIA CIGFTWIASP ACTELEVVML DWLGQMLGLP EQFLARSGGE GGGVIQGTAS
EATLVALLGA KSRTMQKLKE EHPEWTDTEI LGKLVGYCNK QAHSSVERAG LLGGVKLRSL
QPDDKRRLRG DILRKAMDED ISKGLIPFYV VATLGTTSSC TFDALDEIGD VCNERDIWLH
VDAAYAGSAF ICPEYRHFMK GIEKADSFNF NPHKWMLVNF DCSAMWLKQP RWIVDAFNVD
PLYLKHDQQG SAPDYRHWQI PLGRRFRSLK LWFVLRLYGV ENLQKHIRKQ IALAHLFEKH
LGSDERFELF EEVTMGLVCF RLKGSNEINE ELLRRINGRG KIHLVPSKID DVYFLRLAIC
SRFTDDR
//