ID Q964L5_DROPE Unreviewed; 344 AA.
AC Q964L5;
DT 01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT 01-DEC-2001, sequence version 1.
DT 08-NOV-2023, entry version 77.
DE SubName: Full=Alpha methyldopa hypersensitive {ECO:0000313|EMBL:AAK94693.1};
DE Flags: Fragment;
GN Name=amd {ECO:0000313|EMBL:AAK94693.1};
OS Drosophila persimilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7234 {ECO:0000313|EMBL:AAK94693.1};
RN [1] {ECO:0000313|EMBL:AAK94693.1}
RP NUCLEOTIDE SEQUENCE.
RA Tatarenkov A.N., Zurovcova M., Ayala F.J.;
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AAK94693.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=11476641; DOI=10.1006/mpev.2001.0967;
RA Tatarenkov A., Zurovcova M., Ayala F.J.;
RT "Ddc and amd sequences resolve phylogenetic relationships of Drosophila.";
RL Mol. Phylogenet. Evol. 20:321-325(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; AF293720; AAK94693.1; -; Genomic_DNA.
DR AlphaFoldDB; Q964L5; -.
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 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:SF60; 3,4-DIHYDROXYPHENYLACETALDEHYDE SYNTHASE; 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|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR602129-50}.
FT MOD_RES 220
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAK94693.1"
FT NON_TER 344
FT /evidence="ECO:0000313|EMBL:AAK94693.1"
SQ SEQUENCE 344 AA; 37892 MW; FFBE90A2DE8B34FF CRC64;
TSYPSIVGEM LASGFGIIGF SWICSPACTE LEVVVMDWLA KFLKLPEHFQ HASDGPGGGV
IQGSASEAVL VAVLAAREQA VISCKETHPE LSESEVRGKL IAYSSDQSNS CIEKAGVLAA
MPIKLLPADD DLILRGNTLR KAIEDDVAAG LIPVICIATL GTTGTCAYDD IDSLADVCQA
LNVWLHVDAA YAGGGFALEE CTELRRGLDR VDSLNFNLHK FMLVNFDCSA MWLKDANKVV
DSFNVDRIYL KHKHEGQSQI PDFRHWQIPL GRRFRALKVW ITFRTLGAEG LRSHVRKHIA
LAQQFEAFVR NDSRFEMVAP QALGLVCFRP RGDNEHTAQL LQRL
//