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Database: UniProt
Entry: A0A3P8U815_AMPPE
LinkDB: A0A3P8U815_AMPPE
Original site: A0A3P8U815_AMPPE 
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}.
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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
//
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