Reviewed, UniProtKB/Swiss-Prot Q9F5P3 (DCEA_LISMO)

Names and origin

Protein names

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

Gene names

Name:	gadA
Ordered Locus Names:	lmo0447

Organism

Listeria monocytogenes [Complete proteome] [HAMAP]

Taxonomic identifier

1639 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Listeriaceae › Listeria

Protein attributes

Sequence length	462 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Converts internalized glutamate to GABA and increases the internal pH. Involved in glutamate-dependent acid resistance in gastric fluid.
Catalytic activity	L-glutamate = 4-aminobutanoate + CO2.
Cofactor	Pyridoxal phosphate By similarity.
Sequence similarities	Belongs to the group II decarboxylase family.

Ontologies

Keywords
Ligand	Pyridoxal phosphate
Molecular function	Decarboxylase Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glutamate metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	glutamate decarboxylase activity Inferred from electronic annotation. Source: EC 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 alpha		PRO_0000146988
Amino acid modifications
	Modified residue	273	1	N6-(pyridoxal phosphate)lysine By similarity
Experimental info
	Sequence conflict	152	1	S → N in AAG22560. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9F5P3-1 [UniParc]. Last modified February 21, 2002. Version 2. Checksum: EA1A442E3E1CE2FA	FASTA	462	52,498
	10 20 30 40 50 60 MFKTNVEQNN VPVFGSFESG QDLPEKRMNK ESVDPRIAYQ LVKDQLIDEG SARQNLATFC 70 80 90 100 110 120 QTYMEPEAEQ IMAETMEKNA IDKSEYPQTA KLESSCVNML ADLWNVDESE HYMGTSTVGS 130 140 150 160 170 180 SEACMLGGMA MKFRWRSAAL KNGLDIHAKK PSLVISSGYQ VCWEKFCVYW DIELREVPMS 190 200 210 220 230 240 EEHLSINTDI IMDYVDEYTI GIVGILGITY TGKFDDIMTL NDLVEDYNNT HDNEVVIHVD 250 260 270 280 290 300 GASGAMFTPF VEPGLEWDFR LPNVVSINTS GHKYGLVYPG VGWILWRDKE YLPEELVFDV 310 320 330 340 350 360 SYLGGHMPTM AINFSRSASQ IIGQYYNFLR FGYEGYRQIH MRTRDGALQL SQAVAETGLF 370 380 390 400 410 420 EIYNDGANLP IVCYKLKDDA NVAWTLYDLA DRLQMKGWQV PAYPLPKEMG NTIIQRYVCR 430 440 450 460 GDLGQNMVTA FKNDLSESIE ELNNAHILYH DVNTSKTHGF TH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A glutamate decarboxylase system protects Listeria monocytogenes in gastric fluid." Cotter P.D., Gahan C.G.M., Hill C. Mol. Microbiol. 40:465-475(2001) [PubMed: 11309128] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: LO28 / Serovar 1/2c.
[2]	"Comparative genomics of Listeria species." Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E., Dominguez-Bernal G., Duchaud E. , Durant L., Dussurget O., Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P. Science 294:849-852(2001) [PubMed: 11679669] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-679 / EGD-e / Serovar 1/2a.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF309076 Genomic DNA. Translation: AAG22560.1. AL591975 Genomic DNA. Translation: CAC98526.1.
PIR	AH1130.
RefSeq	NP_463976.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	986724.
GenomeReviews	Gene locus lmo0447 in contig AL591824_GR.
KEGG	lmo:lmo0447.
Organism-specific databases
ListiList	LMO00447.
CMR	Search...
Phylogenomic databases
HOGENOM	Q9F5P3.
OMA	NCRDNAT.
Enzyme and pathway databases
BioCyc	LMON169963:LMO0447-MON.
BRENDA	4.1.1.15. 96770.
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...

Entry information

Entry name

DCEA_LISMO

Accession

Primary (citable) accession number: Q9F5P3
Secondary accession number(s): Q8Y9S6

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2002
Last sequence update:	February 21, 2002
Last modified:	November 3, 2009
This is version 47 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)