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Database: UniProt/SWISS-PROT
Entry: GADA_DICDI
LinkDB: GADA_DICDI
Original site: GADA_DICDI 
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   28-FEB-2018, entry version 80.
DE   RecName: Full=Glutamate decarboxylase A;
DE            EC=4.1.1.15;
GN   Name=gadA; ORFNames=DDB_G0280199;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Mycetozoa; Dictyostelids; 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.,
RA   Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q.,
RA   Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F.,
RA   Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P.,
RA   Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P.,
RA   Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N.,
RA   Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M.,
RA   Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I.,
RA   Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R.,
RA   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.,
RA   Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D.,
RA   Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S.,
RA   Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T.,
RA   Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A.,
RA   Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M.,
RA   Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G.,
RA   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
RT   GABAB 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.,
RA   Peracino B., Skelton J., Ivens A., Bozzaro S.;
RT   "Genome-wide transcriptional changes induced by phagocytosis or growth
RT   on bacteria in Dictyostelium.";
RL   BMC Genomics 9:291-291(2008).
CC   -!- FUNCTION: Generates GABA from glutamate. GABA induces the release
CC       of acbA from prespore cells and induces the exposure of tagC on
CC       the surface of prestalk cells where it can convert acbA to SDF-2.
CC       Glutamate acts as a competitive inhibitor.
CC       {ECO:0000269|PubMed:16672332}.
CC   -!- CATALYTIC ACTIVITY: L-glutamate = 4-aminobutanoate + CO(2).
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
CC       in development. {ECO:0000269|PubMed:16672332}.
CC   -!- DEVELOPMENTAL STAGE: Expressed only after 10 hours of development
CC       and its mRNA accumulates to peak at 18 hours when cells are
CC       initiating fruiting body formation. Highly expressed during
CC       phagocytosis of non-pathogenic bacteria.
CC       {ECO:0000269|PubMed:11553701, ECO:0000269|PubMed:18559084}.
CC   -!- DISRUPTION PHENOTYPE: Mutant cells grow and develop well, forming
CC       normally proportioned fruiting bodies, but the number of viable
CC       spores is reduced to about half. {ECO:0000269|PubMed:16672332}.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000305}.
DR   EMBL; AAFI02000035; EAL67326.1; -; Genomic_DNA.
DR   RefSeq; XP_641300.1; XM_636208.1.
DR   ProteinModelPortal; Q54VQ5; -.
DR   SMR; Q54VQ5; -.
DR   STRING; 44689.DDB0231446; -.
DR   PaxDb; Q54VQ5; -.
DR   EnsemblProtists; EAL67326; EAL67326; DDB_G0280199.
DR   GeneID; 8622433; -.
DR   KEGG; ddi:DDB_G0280199; -.
DR   dictyBase; DDB_G0280199; gadA.
DR   eggNOG; KOG1383; Eukaryota.
DR   eggNOG; COG0076; LUCA.
DR   InParanoid; Q54VQ5; -.
DR   KO; K01580; -.
DR   OMA; RPNLVMG; -.
DR   PhylomeDB; Q54VQ5; -.
DR   PRO; PR:Q54VQ5; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   Proteomes; UP000002195; Unassembled WGS sequence.
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; 3.40.640.10; -; 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   PANTHER; PTHR43321; PTHR43321; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01788; Glu-decarb-GAD; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Lyase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN         1    462       Glutamate decarboxylase A.
FT                                /FTId=PRO_0000391329.
FT   REGION      124    125       Pyridoxal phosphate binding.
FT                                {ECO:0000250}.
FT   BINDING      62     62       Substrate. {ECO:0000250}.
FT   BINDING      83     83       Substrate. {ECO:0000250}.
FT   BINDING     210    210       Pyridoxal phosphate. {ECO:0000250}.
FT   BINDING     273    273       Pyridoxal phosphate. {ECO:0000250}.
FT   MOD_RES     274    274       N6-(pyridoxal phosphate)lysine.
FT                                {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
//
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