ID   GADA_DICDI              Reviewed;         462 AA.
AC   Q54VQ5;
DT   09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 100.
DE   RecName: Full=Glutamate decarboxylase A;
DE            EC=4.1.1.15;
GN   Name=gadA; ORFNames=DDB_G0280199;
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [2]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=11553701; DOI=10.1091/mbc.12.9.2590;
RA   Iranfar N., Fuller D., Sasik R., Hwa T., Laub M., Loomis W.F.;
RT   "Expression patterns of cell-type-specific genes in Dictyostelium.";
RL   Mol. Biol. Cell 12:2590-2600(2001).
RN   [3]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=16672332; DOI=10.1242/dev.02399;
RA   Anjard C., Loomis W.F.;
RT   "GABA induces terminal differentiation of Dictyostelium through a GABAB
RT   receptor.";
RL   Development 133:2253-2261(2006).
RN   [4]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=18559084; DOI=10.1186/1471-2164-9-291;
RA   Sillo A., Bloomfield G., Balest A., Balbo A., Pergolizzi B., Peracino B.,
RA   Skelton J., Ivens A., Bozzaro S.;
RT   "Genome-wide transcriptional changes induced by phagocytosis or growth on
RT   bacteria in Dictyostelium.";
RL   BMC Genomics 9:291-291(2008).
CC   -!- FUNCTION: Generates GABA from glutamate. GABA induces the release of
CC       acbA from prespore cells and induces the exposure of tagC on the
CC       surface of prestalk cells where it can convert acbA to SDF-2. Glutamate
CC       acts as a competitive inhibitor. {ECO:0000269|PubMed:16672332}.
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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Exclusively expressed in prespore cells late in
CC       development. {ECO:0000269|PubMed:16672332}.
CC   -!- DEVELOPMENTAL STAGE: Expressed only after 10 hours of development and
CC       its mRNA accumulates to peak at 18 hours when cells are initiating
CC       fruiting body formation. Highly expressed during phagocytosis of non-
CC       pathogenic bacteria. {ECO:0000269|PubMed:11553701,
CC       ECO:0000269|PubMed:18559084}.
CC   -!- DISRUPTION PHENOTYPE: Mutant cells grow and develop well, forming
CC       normally proportioned fruiting bodies, but the number of viable spores
CC       is reduced to about half. {ECO:0000269|PubMed:16672332}.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000305}.
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DR   EMBL; AAFI02000035; EAL67326.1; -; Genomic_DNA.
DR   RefSeq; XP_641300.1; XM_636208.1.
DR   AlphaFoldDB; Q54VQ5; -.
DR   SMR; Q54VQ5; -.
DR   STRING; 44689.Q54VQ5; -.
DR   PaxDb; 44689-DDB0231446; -.
DR   EnsemblProtists; EAL67326; EAL67326; DDB_G0280199.
DR   GeneID; 8622433; -.
DR   KEGG; ddi:DDB_G0280199; -.
DR   dictyBase; DDB_G0280199; gadA.
DR   eggNOG; KOG1383; Eukaryota.
DR   HOGENOM; CLU_019582_2_2_1; -.
DR   InParanoid; Q54VQ5; -.
DR   OMA; RPNLVMG; -.
DR   PhylomeDB; Q54VQ5; -.
DR   PRO; PR:Q54VQ5; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0005829; C:cytosol; IDA:dictyBase.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; ISS:dictyBase.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006538; P:glutamate catabolic process; ISS:dictyBase.
DR   Gene3D; 3.90.1150.160; -; 1.
DR   Gene3D; 4.10.280.50; -; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR010107; Glutamate_decarboxylase.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   NCBIfam; TIGR01788; Glu-decarb-GAD; 1.
DR   PANTHER; PTHR43321; GLUTAMATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43321:SF3; GLUTAMATE DECARBOXYLASE; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   2: Evidence at transcript level;
KW   Lyase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..462
FT                   /note="Glutamate decarboxylase A"
FT                   /id="PRO_0000391329"
FT   BINDING         62
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         83
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         124..125
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         210
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         273
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         274
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   462 AA;  52621 MW;  5DFE4AB49DD215CB CRC64;
     MSLHHVKTNK YKGFYDSYAS PPATKEISKY SLKEESNKPE VIRDLIIDEL LLDGNAKQNL
     ATFCQTDLDK EIHVLMDKCI DKNMIDKDEY PQTAEIESRC VHILADLWNS PESSETIGCS
     TTGSSEAAML GGMALKWRWR ENRKKQGKPF DKPNIVTGPV QICWHKFALY FDIELREVPM
     EHDRYIMTPE EAIKRCDENT IGVIPTLGVT FTLQYEDVKG ISEALDKFEK ETGLDIPIHV
     DAASGGFVAP FLQPEIVWDF RLPRVKSING SGHKFGLSPL GVGWVVWRGK NDIHKDLVFD
     VNYLGGNMPT FSLNFSRPGG QIVCQYYNFL RHGRSGYTAV HQACLDHGIF ISKQVKKHGI
     FDIVYDGTGA LPGACWKLKK DAKVKFNLFD LSDRMRNRGW QIASYTLPNL PDIVVQRVLI
     RHGFSHDMAM LLIEDFNRSI EYFDKHPMVQ SISKDEGQSF HH
//