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Database: UniProt
Entry: Q964L5_DROPE
LinkDB: Q964L5_DROPE
Original site: Q964L5_DROPE 
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
//
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