ID A0A087R0L8_APTFO Unreviewed; 493 AA.
AC A0A087R0L8;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Glutamate decarboxylase 1 {ECO:0000256|ARBA:ARBA00040578};
DE EC=4.1.1.15 {ECO:0000256|ARBA:ARBA00012421};
DE Flags: Fragment;
GN ORFNames=AS27_06858 {ECO:0000313|EMBL:KFM07022.1};
OS Aptenodytes forsteri (Emperor penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC Aptenodytes.
OX NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM07022.1, ECO:0000313|Proteomes:UP000053286};
RN [1] {ECO:0000313|EMBL:KFM07022.1, ECO:0000313|Proteomes:UP000053286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM07022.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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 EMBL; KL226022; KFM07022.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087R0L8; -.
DR STRING; 9233.A0A087R0L8; -.
DR Proteomes; UP000053286; Unassembled WGS sequence.
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:UP000053286}.
FT MOD_RES 304
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFM07022.1"
FT NON_TER 493
FT /evidence="ECO:0000313|EMBL:KFM07022.1"
SQ SEQUENCE 493 AA; 55972 MW; 20CDC02DF73FC5FA CRC64;
DLLPAKNGEE QTMQFLLEVV DILLNYVRKT FDRSTKVLDF HHPHQLLEGM EGFNLELSDN
PESLEQILVD CRDTLKYGVR TGHPRFFNQL STGLDIIGLA GEWLTSTANT NMFTYEIAPV
FVLMEQITLQ KMREIIGWSN KDGDGIFSPG GAISNMYSIM AARYKYFPEV KTKGMAAVPK
LVLFTSEHSH YSIKKAGAAL GFGTDNVILI KCNERGKIIP ADLEAKILEA KQKGYIPLFV
NATAGTTVYG AFDPIQEIAD ICEKYNLWLH VDAAWGGGLL MSRKHRHKLN GIERANSVTW
NPHKMMGVLL QCSAILVREK GILQGCNQMC AGYLFQQDKQ YDVTYDTGDK AIQCGRHVDI
FKFWLMWKAK GTVGFENQIN KCLELAEYLY TKIKNREEFE MVFEGEPEHT NVCFWYIPPS
LRGMPDCDER REKLHRVAPK IKALMMESGT TMVGYQPQGD KVNFFRMVIS NPAATKSDID
FLIEEIERLG QEL
//
