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O30418 (DCE_LACLM) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamate decarboxylase

EC=4.1.1.15
Gene names
Name:gadB
Ordered Locus Names:llmg_1179
OrganismLactococcus lactis subsp. cremoris (strain MG1363) [Complete proteome] [HAMAP]
Taxonomic identifier416870 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeLactococcus

Protein attributes

Sequence length466 AA.
Sequence statusComplete.
Protein existenceEvidence 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
   LigandPyridoxal phosphate
   Molecular functionDecarboxylase
Lyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglutamate metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functionglutamate decarboxylase activity

Inferred from electronic annotation. Source: UniProtKB-EC

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 466466Glutamate decarboxylase
PRO_0000146987

Amino acid modifications

Modified residue2771N6-(pyridoxal phosphate)lysine By similarity

Experimental info

Sequence conflict1141E → G in AAC46188. Ref.1
Sequence conflict116 – 1172FM → IY in AAC46188. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O30418 [UniParc].

Last modified May 1, 2007. Version 2.
Checksum: 668DB73A4DF40BF9

FASTA46653,924
        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 

« Hide

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MG1363.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF005098 Genomic DNA. Translation: AAC46188.1.
AM406671 Genomic DNA. Translation: CAL97772.1.
RefSeqYP_001032492.1. NC_009004.1.

3D structure databases

ProteinModelPortalO30418.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING416870.llmg_1179.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAL97772; CAL97772; llmg_1179.
GeneID4797573.
KEGGllm:llmg_1179.
PATRIC22283506. VBILacLac4574_1210.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0076.
HOGENOMHOG000070228.
KOK01580.
OMAIADLWNA.
OrthoDBEOG6TFCPW.
ProtClustDBCLSK876864.

Enzyme and pathway databases

BioCycLLAC416870:GCDT-1204-MONOMER.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
InterProIPR010107. Glutamate_decarboxylase.
IPR002129. PyrdxlP-dep_de-COase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PANTHERPTHR11999:SF1. PTHR11999:SF1. 1 hit.
PfamPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
SUPFAMSSF53383. SSF53383. 1 hit.
TIGRFAMsTIGR01788. Glu-decarb-GAD. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDCE_LACLM
AccessionPrimary (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: February 19, 2014
This is version 74 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families