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Reviewed, UniProtKB/Swiss-Prot O30418 (DCE_LACLM)

Last modified November 3, 2009. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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 lineageBacteriaFirmicutesLactobacillalesStreptococcaceaeLactococcus

Protein attributes

Sequence length466 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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

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
O30418-1 [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: 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

AF005098 Genomic DNA. Translation: AAC46188.1.
AM406671 Genomic DNA. Translation: CAL97772.1.
RefSeqYP_001032492.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGO30418.

Genome annotation databases

GeneID4797573.
GenomeReviewsGene locus llmg_1179 in contig AM406671_GR.
KEGGllm:llmg_1179.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAAVDEDTI.

Family and domain databases

InterProIPR010107. Glutamate_decarboxylase.
IPR002129. PyrdxlP-dep_de-COase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
PANTHERPTHR11999:SF1. Glu_decarb_GAD. 1 hit.
PTHR11999. Pyridoxal_deC. 1 hit.
PfamPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
TIGRFAMsTIGR01788. Glu-decarb-GAD. 1 hit.
PROSITEPS00392. DDC_GAD_HDC_YDC. False negative.
[Graphical view]
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: November 3, 2009
This is version 49 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents