ID Q8WSC6_9MUSC Unreviewed; 378 AA.
AC Q8WSC6;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 76.
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:AAL37927.1,
GN ECO:0000313|FlyBase:FBgn0046971};
OS Drosophila ellisoni.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=170950 {ECO:0000313|EMBL:AAL37927.1};
RN [1] {ECO:0000313|EMBL:AAL37927.1}
RP NUCLEOTIDE SEQUENCE.
RA Tatarenkov A.N., Ayala F.J.;
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AAL37927.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=11697926; DOI=10.1006/mpev.2001.1002;
RA Tatarenkov A., Ayala F.J.;
RT "Phylogenetic relationships among species groups of the virilis-repleta
RT radiation of Drosophila.";
RL Mol. Phylogenet. Evol. 21:327-331(2001).
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; AF324969; AAL37927.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8WSC6; -.
DR FlyBase; FBgn0046971; Dell\Ddc.
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; 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 3: Inferred from homology;
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 236
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAL37927.1"
FT NON_TER 378
FT /evidence="ECO:0000313|EMBL:AAL37927.1"
SQ SEQUENCE 378 AA; 42120 MW; 9BDFD2EB224A20AA CRC64;
VTHWHSPKFH AYFPTANSYP AIVADMLSGA IACIGFTWIA SPACTELEVV MLDWLGKMLD
LPAEFLACSG GKGGGVIQGT ASESTLVALL GAKAKKIEQV KKEHPEWDDH TIIGKLVGYS
SAQAHSSVER AGLLGGVKLR SVPADEHNRL RGDALEQAIQ EDLAAGLIPF YAVVTLGTTN
SCAFDRLDEC GTVANKHNVW VHVDAAYAGS AFICPEYRHH MKGIETADSF NFNPHKWMLV
NFDCSAMWLK DPSWVVNAFN VDPLYLKHDM QGSAPDYRHW QIPLGRRFRA LKLWFVLRLY
GVENLQAHIR RHCGFAQQFG DLCQADERFE LAAEVNMGLV CFRLKGSNER NEALLKRING
RGNIHMVPAK IRDVYFLR
//
