ID Q8WSC4_9MUSC Unreviewed; 378 AA.
AC Q8WSC4;
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:AAL37929.1,
GN ECO:0000313|FlyBase:FBgn0046960};
OS Drosophila gaucha.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=30028 {ECO:0000313|EMBL:AAL37929.1};
RN [1] {ECO:0000313|EMBL:AAL37929.1}
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:AAL37929.1}
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; AF324971; AAL37929.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8WSC4; -.
DR FlyBase; FBgn0046960; Dgau\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:AAL37929.1"
FT NON_TER 378
FT /evidence="ECO:0000313|EMBL:AAL37929.1"
SQ SEQUENCE 378 AA; 42127 MW; B5B9AA49B1489E32 CRC64;
ITHWHSPKFH AYFPTANSYP AIVADMLSGA IACIGFTWIA SPACTELEVV MLDWLGKMLD
LPAEFLACSG GKGGGVIQGT ASESTLVALL GAKAKKLKQV KEEHPEWDEH TIIGKLVGYA
SAQAHSSVER AGLLGGVKLR SVPADEHNRL RGDALEQAIK EDLAAGLIPF YAVVTLGTTN
SCAFDRLDEC GPVANKHNVW VHVDAAYAGS AFICPEYRHH MKGIETADSF NFNPHKWMLV
NFDCSAMWLK DPSWVVNAFN VDPLYLKHDM QGSAPDYRHW QIPLGRRFRA LKLWFVLRLY
GVENLQAHIR RHCGFAQQFG DLCQQDARFE LAAEVNMGLV CFRLKGSNER NEALLKRING
RGNIHMVPAK IRDVYFLR
//
