ID   G5EDB7_CAEEL            Unreviewed;       508 AA.
AC   G5EDB7;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   SubName: Full=Glutamate decarboxylase 1 {ECO:0000313|EMBL:CAA21537.1};
DE   SubName: Full=Glutamic acid decarboxylase {ECO:0000313|EMBL:AAD19958.1};
GN   Name=unc-25 {ECO:0000313|EMBL:CAA21537.1,
GN   ECO:0000313|WormBase:Y37D8A.23a};
GN   ORFNames=CELE_Y37D8A.23 {ECO:0000313|EMBL:CAA21537.1}, Y37D8A.23
GN   {ECO:0000313|WormBase:Y37D8A.23a};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000313|EMBL:AAD19958.1};
RN   [1] {ECO:0000313|EMBL:CAA21537.1, ECO:0000313|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000313|EMBL:CAA21537.1,
RC   ECO:0000313|Proteomes:UP000001940};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RA   Sulson J.E., Waterston R.;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2] {ECO:0000313|EMBL:AAD19958.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Bristol {ECO:0000313|EMBL:AAD19958.1};
RX   PubMed=9880574;
RA   Jin Y., Jorgensen E., Hartwieg E., Horvitz H.R.;
RT   "The Caenorhabditis elegans gene unc-25 encodes glutamic acid decarboxylase
RT   and is required for synaptic transmission but not synaptic development.";
RL   J. Neurosci. 19:539-548(1999).
RN   [3] {ECO:0000313|EMBL:CAA21537.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Bristol N2 {ECO:0000313|EMBL:CAA21537.1};
RA   Sulson J.E., Waterston R.;
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:CAA21537.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Bristol N2 {ECO:0000313|EMBL:CAA21537.1};
RG   WormBase Consortium;
RA   WormBase;
RL   Submitted (AUG-2023) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU000382}.
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DR   EMBL; AF109378; AAD19958.1; -; mRNA.
DR   EMBL; BX284603; CAA21537.1; -; Genomic_DNA.
DR   PIR; T26636; T26636.
DR   RefSeq; NP_499689.1; NM_067288.4.
DR   SMR; G5EDB7; -.
DR   STRING; 6239.Y37D8A.23a.1; -.
DR   PaxDb; 6239-Y37D8A-23a; -.
DR   EnsemblMetazoa; Y37D8A.23a.1; Y37D8A.23a.1; WBGene00006762.
DR   GeneID; 176713; -.
DR   KEGG; cel:CELE_Y37D8A.23; -.
DR   AGR; WB:WBGene00006762; -.
DR   WormBase; Y37D8A.23a; CE20226; WBGene00006762; unc-25.
DR   eggNOG; KOG0629; Eukaryota.
DR   OMA; RHATYHA; -.
DR   OrthoDB; 888358at2759; -.
DR   Reactome; R-CEL-888568; GABA synthesis.
DR   Reactome; R-CEL-888590; GABA synthesis, release, reuptake and degradation.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00006762; Expressed in larva and 3 other cell types or tissues.
DR   GO; GO:0030424; C:axon; IDA:WormBase.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0060077; C:inhibitory synapse; IDA:WormBase.
DR   GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
DR   GO; GO:0043204; C:perikaryon; IDA:UniProtKB.
DR   GO; GO:0008021; C:synaptic vesicle; IDA:WormBase.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; ISS:WormBase.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; ISS:WormBase.
DR   GO; GO:0009449; P:gamma-aminobutyric acid biosynthetic process; ISS:WormBase.
DR   GO; GO:0051932; P:synaptic transmission, GABAergic; IGI:WormBase.
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   PANTHER; PTHR45677:SF10; GLUTAMATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   1: Evidence at protein level;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW   Proteomics identification {ECO:0007829|EPD:G5EDB7,
KW   ECO:0007829|PeptideAtlas:G5EDB7};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001940}.
FT   MOD_RES         320
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   508 AA;  57793 MW;  592DE1381ADF02AB CRC64;
     MSSAAADESD AVLENLIAKE ILPQTGNWEG TEEFLNRIVQ VLLKYIKDQN DRDQKILEFH
     HPDKMQMLMD LSIPEKPESL LKLVKSCEDV LRLGVRTGHP RFFNQISCGL DLVSMAGEWL
     TATANTNMFT YEIAPVFILM EKSVMARMWE AVGWDPEKAD GIFAPGGAIA NLYAMNAARH
     QLWPRSKHLG MKDIPTLCCF TSEDSHYSIK SASAVLGIGA DYCFNIPTDK NGKMIPEALE
     AKIIECKKEG LTPFFACCTA GSTVYGAFDP LERVANICER HKLWFHVDAA WGGGMLLSPE
     HRYKLAGIER ANSVTWNPHK LMGALLQCSA CLFRQDGLLF QCNQMSADYL FQQDKPYDVS
     FDTGDKAIQC GRHNDVFKLW LMWKSKGMEG YRQQINKLMD LANYFTRRIK ETEGFELIIE
     NPEFLNICFW YVPSKIRNLE PAEMRARLEK IAPKIKAGMM QRGTTMVGYQ PDKQRPNFFR
     MIISNQAITR EDLDFLIKEI VDIGESLE
//