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Protein

Glutamate decarboxylase

Gene

gadB

Organism
Lactococcus lactis subsp. cremoris (strain MG1363)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Converts internalized glutamate to GABA and increases the internal pH. Involved in glutamate-dependent acid resistance.

Catalytic activityi

L-glutamate = 4-aminobutanoate + CO2.

Cofactori

GO - Molecular functioni

  1. glutamate decarboxylase activity Source: UniProtKB-EC
  2. pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  1. glutamate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciLLAC416870:GCDT-1204-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate decarboxylase (EC:4.1.1.15)
Gene namesi
Name:gadB
Ordered Locus Names:llmg_1179
OrganismiLactococcus lactis subsp. cremoris (strain MG1363)
Taxonomic identifieri416870 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeLactococcus
ProteomesiUP000000364 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 466466Glutamate decarboxylasePRO_0000146987Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei277 – 2771N6-(pyridoxal phosphate)lysineBy similarity

Expressioni

Inductioni

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.

Interactioni

Protein-protein interaction databases

STRINGi416870.llmg_1179.

Structurei

3D structure databases

ProteinModelPortaliO30418.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the group II decarboxylase family.Curated

Phylogenomic databases

eggNOGiCOG0076.
HOGENOMiHOG000070228.
KOiK01580.
OMAiDPDLVWD.
OrthoDBiEOG6TFCPW.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
InterProiIPR010107. Glutamate_decarboxylase.
IPR002129. PyrdxlP-dep_de-COase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PANTHERiPTHR11999:SF1. PTHR11999:SF1. 1 hit.
PfamiPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01788. Glu-decarb-GAD. 1 hit.

Sequencei

Sequence statusi: Complete.

O30418-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLYGKENRDE AEFLEPIFGS ESEQVDLPKY KLAQQSIEPR VAYQLVQDEM
60 70 80 90 100
LDEGNARLNL ATFCQTYMEP EAVKLMSQTL EKNAIDKSEY PRTTEIENRC
110 120 130 140 150
VNMIADLWNA SEKEKFMGTS TIGSSEACML GGMAMKFSWR KRAEKLGLDI
160 170 180 190 200
NAKKPNLVIS SGYQVCWEKF CVYWDIEMRE VPMDREHMSI NLEKVMDYVD
210 220 230 240 250
EYTIGVVGIM GITYTGRYDD IKALDNLIEE YNKQTDYKVY IHVDAASGGL
260 270 280 290 300
YAPFVEPELE WDFRLKNVIS INTSGHKYGL VYPGVGWVLW RDKKYLPEEL
310 320 330 340 350
IFKVSYLGGE LPTMAINFSH SASQLIGQYY NFVRYGFDGY KAIHERTHKV
360 370 380 390 400
AMYLAEEIEK TGMFEIMNDG AQLPIVCYKL KENSNRGWNL YDLADRLLMK
410 420 430 440 450
GWQVPAYPLP KNLENEIIQR LVIRADFGMN MAFNYVQDMQ EAIDALNKAH
460
ILFHQEPENK TYGFTH
Length:466
Mass (Da):53,924
Last modified:May 1, 2007 - v2
Checksum:i668DB73A4DF40BF9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti114 – 1141E → G in AAC46188 (PubMed:9484886).Curated
Sequence conflicti116 – 1172FM → IY in AAC46188 (PubMed:9484886).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF005098 Genomic DNA. Translation: AAC46188.1.
AM406671 Genomic DNA. Translation: CAL97772.1.
RefSeqiYP_001032492.1. NC_009004.1.

Genome annotation databases

EnsemblBacteriaiCAL97772; CAL97772; llmg_1179.
GeneIDi4797573.
KEGGillm:llmg_1179.
PATRICi22283506. VBILacLac4574_1210.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF005098 Genomic DNA. Translation: AAC46188.1.
AM406671 Genomic DNA. Translation: CAL97772.1.
RefSeqiYP_001032492.1. NC_009004.1.

3D structure databases

ProteinModelPortaliO30418.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi416870.llmg_1179.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAL97772; CAL97772; llmg_1179.
GeneIDi4797573.
KEGGillm:llmg_1179.
PATRICi22283506. VBILacLac4574_1210.

Phylogenomic databases

eggNOGiCOG0076.
HOGENOMiHOG000070228.
KOiK01580.
OMAiDPDLVWD.
OrthoDBiEOG6TFCPW.

Enzyme and pathway databases

BioCyciLLAC416870:GCDT-1204-MONOMER.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
InterProiIPR010107. Glutamate_decarboxylase.
IPR002129. PyrdxlP-dep_de-COase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PANTHERiPTHR11999:SF1. PTHR11999:SF1. 1 hit.
PfamiPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01788. Glu-decarb-GAD. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1997) [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(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MG1363.

Entry informationi

Entry nameiDCE_LACLM
AccessioniPrimary (citable) accession number: O30418
Secondary accession number(s): A2RKG2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: May 1, 2007
Last modified: March 4, 2015
This is version 80 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.