ID A0A3P9P3Q0_POERE Unreviewed; 510 AA.
AC A0A3P9P3Q0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Acidic amino acid decarboxylase GADL1 {ECO:0000313|Ensembl:ENSPREP00000016451.1};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000016451.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000016451.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000016451.1};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|ARBA:ARBA00009533, ECO:0000256|RuleBase:RU000382}.
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DR AlphaFoldDB; A0A3P9P3Q0; -.
DR STRING; 8081.ENSPREP00000016451; -.
DR Ensembl; ENSPRET00000016630.1; ENSPREP00000016451.1; ENSPREG00000011095.1.
DR GeneTree; ENSGT00940000158391; -.
DR OMA; NNHAYEG; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR Bgee; ENSPREG00000011095; Expressed in caudal fin and 1 other cell type or tissue.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR CDD; cd06450; DOPA_deC_like; 1.
DR Gene3D; 3.90.1150.170; -; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR021115; Pyridoxal-P_BS.
DR PANTHER; PTHR45677:SF1; ACIDIC AMINO ACID DECARBOXYLASE GADL1; 1.
DR PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE 3: Inferred from homology;
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382};
KW Reference proteome {ECO:0000313|Proteomes:UP000242638}.
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 322
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 510 AA; 57810 MW; E924BE9B68FEBC56 CRC64;
MASSTETHIK GKMQHFSSHN DPLDRPPLDF AATESFLQQS MTMILEDAVK KATDVRQKVC
EWHSPEELKE LLDLELRDSG EPEARILERC RDAIRYSVKT THPHFFNQLY AGLEPYSLVA
SFITDALKPS LYTYEMSPVF TLMENAVLRK LIQIVGWEEG GDGLFNAGGS MSNMYAMNLA
RYRNFPEIKE LGNSAAPRLA VFTSQECHYS ISKAAALMGI GTKNVFVVPS DKKGKMIPSA
LEEQIESLKS EGGVPFMVNA TAGTTVLGAF DPIDEIADVC EKYKLWLHVD ACWGGAVLMS
NKHKLLMKGI HRVDSVAWNP HKMLMACLQC SAFLVRDKTR LLQRCHSARA SYLFQQDKFY
DVSYDTGDKS VQCSRKPDAF KFWLMWKALG TSELEQRVDR ALAMARYLAD EITKREGFRL
LMEPEYANVC FWYIPPSLRD LPDGPVLQEK LHNVAPVVKE RMMKKGSMMV GYQPHRGQAN
FFRMVVISPQ VSRQDMDFVL DEIHSLGKDL
//
