Reviewed, UniProtKB/Swiss-Prot O30418 (DCE_LACLM)

Names and origin

Protein names

Recommended name:
    Glutamate decarboxylase
    EC=4.1.1.15

Gene names

Name:	gadB
Ordered Locus Names:	llmg_1179

Organism

Lactococcus lactis subsp. cremoris (strain MG1363) [Complete proteome] [HAMAP]

Taxonomic identifier

416870 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Streptococcaceae › Lactococcus

Protein attributes

Sequence length	466 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Converts internalized glutamate to GABA and increases the internal pH. Involved in glutamate-dependent acid resistance.
Catalytic activity	L-glutamate = 4-aminobutanoate + CO2.
Cofactor	Pyridoxal phosphate By similarity.
Induction	Expression is highest at onset of stationary phase in presence of NaCl and glutamate, and at low pH. Chloride-dependent expression is activated by gadR.
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 – 466	466	Glutamate decarboxylase		PRO_0000146987
Amino acid modifications
	Modified residue	277	1	N6-(pyridoxal phosphate)lysine By similarity
Experimental info
	Sequence conflict	114	1	E → G in AAC46188. Ref.1
	Sequence conflict	116 – 117	2	FM → IY in AAC46188. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O30418-1 [UniParc]. Last modified May 1, 2007. Version 2. Checksum: 668DB73A4DF40BF9	FASTA	466	53,924
	10 20 30 40 50 60 MLYGKENRDE AEFLEPIFGS ESEQVDLPKY KLAQQSIEPR VAYQLVQDEM LDEGNARLNL 70 80 90 100 110 120 ATFCQTYMEP EAVKLMSQTL EKNAIDKSEY PRTTEIENRC VNMIADLWNA SEKEKFMGTS 130 140 150 160 170 180 TIGSSEACML GGMAMKFSWR KRAEKLGLDI NAKKPNLVIS SGYQVCWEKF CVYWDIEMRE 190 200 210 220 230 240 VPMDREHMSI NLEKVMDYVD EYTIGVVGIM GITYTGRYDD IKALDNLIEE YNKQTDYKVY 250 260 270 280 290 300 IHVDAASGGL YAPFVEPELE WDFRLKNVIS INTSGHKYGL VYPGVGWVLW RDKKYLPEEL 310 320 330 340 350 360 IFKVSYLGGE LPTMAINFSH SASQLIGQYY NFVRYGFDGY KAIHERTHKV AMYLAEEIEK 370 380 390 400 410 420 TGMFEIMNDG AQLPIVCYKL KENSNRGWNL YDLADRLLMK GWQVPAYPLP KNLENEIIQR 430 440 450 460 LVIRADFGMN MAFNYVQDMQ EAIDALNKAH ILFHQEPENK TYGFTH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A chloride-inducible acid resistance mechanism in Lactococcus lactis and its regulation." Sanders J.W., Leenhouts K., Burghoorn J., Brands J.R., Venema G., Kok J. Mol. Microbiol. 27:299-310(1998) [PubMed: 9484886] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
[2]	"The complete genome sequence of the lactic acid bacterial paradigm Lactococcus lactis subsp. cremoris MG1363." Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C., Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P., van Sinderen D., Kok J. J. Bacteriol. 189:3256-3270(2007) [PubMed: 17307855] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF005098 Genomic DNA. Translation: AAC46188.1. AM406671 Genomic DNA. Translation: CAL97772.1.
RefSeq	YP_001032492.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	O30418.
Genome annotation databases
GeneID	4797573.
GenomeReviews	Gene locus llmg_1179 in contig AM406671_GR.
KEGG	llm:llmg_1179.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	AVDEDTI.
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

DCE_LACLM

Accession

Primary (citable) accession number: O30418
Secondary accession number(s): A2RKG2

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2001
Last sequence update:	May 1, 2007
Last modified:	November 3, 2009
This is version 49 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)