Reviewed, UniProtKB/Swiss-Prot Q04792 (DCE_YEAST)

Names and origin

Protein names

Recommended name:
    Glutamate decarboxylase
      Short name=GAD
    EC=4.1.1.15

Gene names

Name:	GAD1
Ordered Locus Names:	YMR250W
ORF Names:	YM9920.04

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	585 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	L-glutamate = 4-aminobutanoate + CO2.
Cofactor	Pyridoxal phosphate By similarity.
Miscellaneous	Present with 1200 molecules/cell in log phase SD medium. Ref.2
Sequence similarities	Belongs to the group II decarboxylase family.

Ontologies

Keywords
Ligand	Pyridoxal phosphate
Molecular function	Decarboxylase Lyase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glutamate catabolic process Inferred from physical interaction. Source: SGD response to oxidative stress Inferred from mutant phenotype. Source: SGD
Cellular component	cytoplasm Inferred from direct assay. Source: SGD
Molecular function	glutamate decarboxylase activity Inferred from physical interaction. Source: SGD identical protein binding Inferred from physical interaction. Source: IntAct pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-5668,EBI-5668
RNR1	P21524	1	EBI-5668,EBI-15234
RNR2	P09938	1	EBI-5668,EBI-15240

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 585	585	Glutamate decarboxylase		PRO_0000146977
Amino acid modifications
	Modified residue	258	1	Phosphoserine Ref.3
	Modified residue	318	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q04792-1 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: DDD22868CEB7B955	FASTA	585	65,990
	10 20 30 40 50 60 MLHRHGSKQK NFENIAGKVV HDLAGLQLLS NDVQKSAVQS GHQGSNNMRD TSSQGMANKY 70 80 90 100 110 120 SVPKKGLPAD LSYQLIHNEL TLDGNPHLNL ASFVNTFTTD QARKLIDENL TKNLADNDEY 130 140 150 160 170 180 PQLIELTQRC ISMLAQLWHA NPDEEPIGCA TTGSSEAIML GGLAMKKRWE HRMKNAGKDA 190 200 210 220 230 240 SKPNIIMSSA CQVALEKFTR YFEVECRLVP VSHRSHHMLD PESLWDYVDE NTIGCFVILG 250 260 270 280 290 300 TTYTGHLENV EKVADVLSQI EAKHPDWSNT DIPIHADGAS GGFIIPFGFE KEHMKAYGME 310 320 330 340 350 360 RWGFNHPRVV SMNTSGHKFG LTTPGLGWVL WRDESLLADE LRFKLKYLGG VEETFGLNFS 370 380 390 400 410 420 RPGFQVVHQY FNFVSLGHSG YRTQFQNSLF VARAFSFELL NSSKLPGCFE IVSSIHESIE 430 440 450 460 470 480 NDSAPKSVKD YWEHPQAYKP GVPLVAFKLS KKFHEEYPEV PQAILSSLLR GRGWIIPNYP 490 500 510 520 530 540 LPKATDGSDE KEVLRVVFRS EMKLDLAQLL IVDIESILTK LIHSYEKVCH HIELASEQTP 550 560 570 580 ERKSSFIYEM LLALASPQDD IPTPDEIEKK NKLKETTTRN YRGTC

References

[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII." Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. , Skelton J., Walsh S.V., Whitehead S., Barrell B.G. Nature 387:90-93(1997) [PubMed: 9169872] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[3]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z48639 Genomic DNA. Translation: CAA88577.1.
PIR	S53072.
RefSeq	NP_013976.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:2552N.
IntAct	Q04792. 7 interactions.
STRING	Q04792.
Proteomic databases
PeptideAtlas	Q04792.
PRIDE	Q04792.
Genome annotation databases
Ensembl	YMR250W; YMR250W; YMR250W; Saccharomyces cerevisiae. [Genome view]
GeneID	855291.
GenomeReviews	Gene locus YMR250W in contig Z71257_GR.
KEGG	sce:YMR250W.
NMPDR	fig|4932.3.peg.5032.
Organism-specific databases
CYGD	YMR250w.
SGD	S000004862. GAD1.
Phylogenomic databases
HOGENOM	Q04792.
OMA	ELHYLGG.
Enzyme and pathway databases
BRENDA	4.1.1.15. 250.
Gene expression databases
ArrayExpress	Q04792.
Genevestigator	Q04792.
GermOnline	YMR250W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR010107. Glutamate_decarboxylase. IPR002129. PyrdxlP-dep_de-COase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
PANTHER	PTHR11999:SF1. Glu_decarb_GAD. 1 hit. PTHR11999. Pyridoxal_deC. 1 hit.
Pfam	PF00282. Pyridoxal_deC. 1 hit. [Graphical view]
TIGRFAMs	TIGR01788. Glu-decarb-GAD. 1 hit.
PROSITE	PS00392. DDC_GAD_HDC_YDC. False negative. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	978940.

Entry information

Entry name

DCE_YEAST

Accession

Primary (citable) accession number: Q04792

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	November 3, 2009
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)