Q54VQ5 (GADA_DICDI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutamate decarboxylase A
EC=4.1.1.15

Gene names

Name:	gadA
ORF Names:	DDB_G0280199

Organism

Dictyostelium discoideum (Slime mold) [Reference proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	462 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Generates GABA from glutamate. GABA induces the release of acbA from prespore cells and induces the exposure of tagC on the surface of prestalk cells where it can convert acbA to SDF-2. Glutamate acts as a competitive inhibitor. Ref.3
Catalytic activity	L-glutamate = 4-aminobutanoate + CO2.
Cofactor	Pyridoxal phosphate By similarity.
Subunit structure	Homohexamer By similarity.
Tissue specificity	Exclusively expressed in prespore cells late in development. Ref.3
Developmental stage	Expressed only after 10 hours of development and its mRNA accumulates to peak at 18 hours when cells are initiating fruiting body formation. Highly expressed during phagocytosis of non-pathogenic bacteria. Ref.2 Ref.4
Disruption phenotype	Mutant cells grow and develop well, forming normally proportioned fruiting bodies, but the number of viable spores is reduced to about half. Ref.3
Sequence similarities	Belongs to the group II decarboxylase family.

Ontologies

Keywords
Ligand	Pyridoxal phosphate
Molecular function	Lyase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glutamate catabolic process Inferred from sequence or structural similarity. Source: dictyBase
Molecular_function	glutamate decarboxylase activity Inferred from sequence or structural similarity. Source: dictyBase pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 462	462	Glutamate decarboxylase A		PRO_0000391329
Regions
	Region	124 – 125	2	Pyridoxal phosphate binding By similarity
Sites
	Binding site	62	1	Substrate By similarity
	Binding site	83	1	Substrate By similarity
	Binding site	210	1	Pyridoxal phosphate By similarity
	Binding site	273	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	274	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q54VQ5 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: 5DFE4AB49DD215CB	FASTA	462	52,621
	10 20 30 40 50 60 MSLHHVKTNK YKGFYDSYAS PPATKEISKY SLKEESNKPE VIRDLIIDEL LLDGNAKQNL 70 80 90 100 110 120 ATFCQTDLDK EIHVLMDKCI DKNMIDKDEY PQTAEIESRC VHILADLWNS PESSETIGCS 130 140 150 160 170 180 TTGSSEAAML GGMALKWRWR ENRKKQGKPF DKPNIVTGPV QICWHKFALY FDIELREVPM 190 200 210 220 230 240 EHDRYIMTPE EAIKRCDENT IGVIPTLGVT FTLQYEDVKG ISEALDKFEK ETGLDIPIHV 250 260 270 280 290 300 DAASGGFVAP FLQPEIVWDF RLPRVKSING SGHKFGLSPL GVGWVVWRGK NDIHKDLVFD 310 320 330 340 350 360 VNYLGGNMPT FSLNFSRPGG QIVCQYYNFL RHGRSGYTAV HQACLDHGIF ISKQVKKHGI 370 380 390 400 410 420 FDIVYDGTGA LPGACWKLKK DAKVKFNLFD LSDRMRNRGW QIASYTLPNL PDIVVQRVLI 430 440 450 460 RHGFSHDMAM LLIEDFNRSI EYFDKHPMVQ SISKDEGQSF HH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.
[2]	"Expression patterns of cell-type-specific genes in Dictyostelium." Iranfar N., Fuller D., Sasik R., Hwa T., Laub M., Loomis W.F. Mol. Biol. Cell 12:2590-2600(2001) [PubMed] [Europe PMC] [Abstract] Cited for: DEVELOPMENTAL STAGE.
[3]	"GABA induces terminal differentiation of Dictyostelium through a GABAB receptor." Anjard C., Loomis W.F. Development 133:2253-2261(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
[4]	"Genome-wide transcriptional changes induced by phagocytosis or growth on bacteria in Dictyostelium." Sillo A., Bloomfield G., Balest A., Balbo A., Pergolizzi B., Peracino B., Skelton J., Ivens A., Bozzaro S. BMC Genomics 9:291-291(2008) [PubMed] [Europe PMC] [Abstract] Cited for: DEVELOPMENTAL STAGE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAFI02000035 Genomic DNA. Translation: EAL67326.1.
RefSeq	XP_641300.1. XM_636208.1.
3D structure databases
ProteinModelPortal	Q54VQ5.
SMR	Q54VQ5. Positions 18-447.
ModBase	Search...
Protein-protein interaction databases
STRING	44689.DDB_0231446.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0231446; DDB0231446; DDB_G0280199.
GeneID	8622433.
KEGG	ddi:DDB_G0280199.
Organism-specific databases
dictyBase	DDB_G0280199. gadA.
Phylogenomic databases
eggNOG	COG0076.
InParanoid	Q54VQ5.
KO	K01580.
OMA	IELREVP.
ProtClustDB	CLSZ2728831.
Family and domain databases
Gene3D	3.40.640.10. 1 hit.
InterPro	IPR010107. Glutamate_decarboxylase. IPR002129. PyrdxlP-dep_de-COase. IPR015424. PyrdxlP-dep_Trfase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. [Graphical view]
PANTHER	PTHR11999:SF1. PTHR11999:SF1. 1 hit.
Pfam	PF00282. Pyridoxal_deC. 1 hit. [Graphical view]
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMs	TIGR01788. Glu-decarb-GAD. 1 hit.
PROSITE	PS00392. DDC_GAD_HDC_YDC. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GADA_DICDI

Accession

Primary (citable) accession number: Q54VQ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 9, 2010
Last sequence update:	May 24, 2005
Last modified:	May 1, 2013
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)