ID A0A3P8U815_AMPPE Unreviewed; 583 AA.
AC A0A3P8U815;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Glutamate decarboxylase 1 {ECO:0000256|ARBA:ARBA00040578};
DE EC=4.1.1.15 {ECO:0000256|ARBA:ARBA00012421};
OS Amphiprion percula (Orange clownfish) (Lutjanus percula).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=161767 {ECO:0000313|Ensembl:ENSAPEP00000031473.1, ECO:0000313|Proteomes:UP000265080};
RN [1] {ECO:0000313|Ensembl:ENSAPEP00000031473.1, ECO:0000313|Proteomes:UP000265080}
RP NUCLEOTIDE SEQUENCE.
RA Lehmann R.;
RT "Finding Nemo's genes: A chromosome-scale reference assembly of the genome
RT of the orange clownfish Amphiprion percula.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPEP00000031473.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Catalyzes the synthesis of the inhibitory neurotransmitter
CC gamma-aminobutyric acid (GABA) with pyridoxal 5'-phosphate as cofactor.
CC {ECO:0000256|ARBA:ARBA00037700}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-glutamate = 4-aminobutanoate + CO2;
CC Xref=Rhea:RHEA:17785, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:59888; EC=4.1.1.15;
CC Evidence={ECO:0000256|ARBA:ARBA00036502};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17786;
CC Evidence={ECO:0000256|ARBA:ARBA00036502};
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}.
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 AlphaFoldDB; A0A3P8U815; -.
DR STRING; 161767.ENSAPEP00000031473; -.
DR Ensembl; ENSAPET00000032306.1; ENSAPEP00000031473.1; ENSAPEG00000022328.1.
DR GeneTree; ENSGT00940000155526; -.
DR Proteomes; UP000265080; Chromosome 10.
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:SF5; GLUTAMATE DECARBOXYLASE 1; 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 Neurotransmitter biosynthesis {ECO:0000256|ARBA:ARBA00022979};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382};
KW Reference proteome {ECO:0000313|Proteomes:UP000265080}.
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 394
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 583 AA; 65487 MW; E4E9F2039FD2E707 CRC64;
MATSEPRATG GDQDPNSANL RPPSGTYEYA WMHGCTRKLG MKICGFLQKN NSLDEKGRLA
GQKNLLSCDN SDRDARFRHT ETDFSNLFAR DLLPAKNGEE PTIQFLLEVV DILTNYVKKT
FDRSTKVLDF HHPHQLLEGM EGFNLELSDQ PESLEQILVD CRDTLKYGVR TGHPRFFNQL
SSGLDIIGLA GEWLTSTANT NMFTYEIAPV FVLMEQLTLK KMREMIGWPG GEGDGLFSPG
GAISNMYSVM IARYKYFPEV KTKGMSAAPR LVLFTSEHSH YSIKKAGAAL GFGTENVILL
STDERGRVIP ADLEAKIIDA KQKGYVPLFV NATAGSTVYG AFDPINEIAD ICEKYNLWLH
VDGAWGGGLL MSRQHRHKLS GVERANSVTW NPHKMMGVPL QCSAILVREK GILAGCNSMC
AGYLFQPDKQ YDVTYDTGDK AIQCGRHVDI FKFWLMWKAK GTIGFEQHID KCLDLSQYLY
NKIKNREGYE MVFDGVPQHT NVCFWYIPPS LRGMPDGDER REKLHRVAPK IKAMMMESGT
TMVGYQPQGT KVNFFRMVVS NSAATQSDID FLIDEIERLG HDL
//