ID Q8WSB7_9MUSC Unreviewed; 378 AA.
AC Q8WSB7;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 77.
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:AAL37936.1,
GN ECO:0000313|FlyBase:FBgn0046933};
OS Drosophila repletoides.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=170952 {ECO:0000313|EMBL:AAL37936.1};
RN [1] {ECO:0000313|EMBL:AAL37936.1}
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:AAL37936.1}
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}.
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; AF324978; AAL37936.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8WSB7; -.
DR FlyBase; FBgn0046933; Drel\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:AAL37936.1"
FT NON_TER 378
FT /evidence="ECO:0000313|EMBL:AAL37936.1"
SQ SEQUENCE 378 AA; 42154 MW; 2EF89B72E356D906 CRC64;
ITHWHSPKFH AYFPTANSYP AIVADMLSGA IACIGFTWIA SPACTELEVV MLDWLGKMLD
LPAEFLACSG GKGGGVIQGT ASESTLVALL GAKAKKLQQV KAEHPEWDEH TIIGKLVGYA
SAQAHSSVER AGLLGGVKLR SVPADEHNRL RGDALEEAIK QDLADGLIPF YAVVTLGTTN
SCAFDRLDEC GAVANKHNVW VHVDAAYAGS AFICPEYRHH MKGIETADSF NFNPHKWMLV
NFDCSAMWLK DPSWVVNAFN VDPLYLKHDM QGSAPDYRHW QIPLGRRFRA LKLWFVLRLY
GVENLQAHIR RHCGFAKQFG ELCVEDKRFE LAAEVNMGLV CFRLKGSNER NEALLKRING
RGHIHMVPAK IRDVYFLR
//
