ID   Q8AXK3_LEUER            Unreviewed;       182 AA.
AC   Q8AXK3;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   24-JAN-2024, entry version 59.
DE   RecName: Full=Glutamate decarboxylase 1 {ECO:0000256|ARBA:ARBA00040578};
DE   Flags: Fragment;
OS   Leucoraja erinacea (Little skate) (Raja erinacea).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Batoidea; Rajiformes; Rajidae; Leucoraja.
OX   NCBI_TaxID=7782 {ECO:0000313|EMBL:AAN61945.1};
RN   [1] {ECO:0000313|EMBL:AAN61945.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=12446824;
RA   Lariviere K., MacEachern L., Greco V., Majchrzak G., Chiu S., Drouin G.,
RA   Trudeau V.L.;
RT   "GAD(65) and GAD(67) isoforms of the glutamic acid decarboxylase gene
RT   originated before the divergence of cartilaginous fishes.";
RL   Mol. Biol. Evol. 19:2325-2329(2002).
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|RuleBase:RU000382};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU000382}.
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DR   EMBL; AF432149; AAN61945.1; -; mRNA.
DR   AlphaFoldDB; Q8AXK3; -.
DR   GO; GO:0016830; F:carbon-carbon lyase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
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   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.
PE   2: Evidence at transcript level;
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|RuleBase:RU000382}.
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAN61945.1"
FT   NON_TER         182
FT                   /evidence="ECO:0000313|EMBL:AAN61945.1"
SQ   SEQUENCE   182 AA;  20020 MW;  786E190B6A966312 CRC64;
     IAPVFVLMEQ ITLKKMREII GWPNGDGDGI FSPGGAISNM YSIMAARYQY FPDVKSKGMT
     AVPKLVLFTS ENSHYSIKKA GAALGFGTDH VILLKCDERG KIMPADLETK IIETKQKGYI
     PIYVNATAGN TVYGAFDPIE EIADVCAKYN LWLHVDAAWG GGLLMSRKHR HKLNGIERAN
     SV
//