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O30418

- DCE_LACLM

UniProt

O30418 - DCE_LACLM

Protein

Glutamate decarboxylase

Gene

gadB

Organism
Lactococcus lactis subsp. cremoris (strain MG1363)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 76 (01 Oct 2014)
      Sequence version 2 (01 May 2007)
      Previous versions | rss
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    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

    Pyridoxal phosphate.By similarity

    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

    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: 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.
    OMAiPTFQINF.
    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

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    MLYGKENRDE AEFLEPIFGS ESEQVDLPKY KLAQQSIEPR VAYQLVQDEM    50
    LDEGNARLNL ATFCQTYMEP EAVKLMSQTL EKNAIDKSEY PRTTEIENRC 100
    VNMIADLWNA SEKEKFMGTS TIGSSEACML GGMAMKFSWR KRAEKLGLDI 150
    NAKKPNLVIS SGYQVCWEKF CVYWDIEMRE VPMDREHMSI NLEKVMDYVD 200
    EYTIGVVGIM GITYTGRYDD IKALDNLIEE YNKQTDYKVY IHVDAASGGL 250
    YAPFVEPELE WDFRLKNVIS INTSGHKYGL VYPGVGWVLW RDKKYLPEEL 300
    IFKVSYLGGE LPTMAINFSH SASQLIGQYY NFVRYGFDGY KAIHERTHKV 350
    AMYLAEEIEK TGMFEIMNDG AQLPIVCYKL KENSNRGWNL YDLADRLLMK 400
    GWQVPAYPLP KNLENEIIQR LVIRADFGMN MAFNYVQDMQ EAIDALNKAH 450
    ILFHQEPENK TYGFTH 466
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF005098 Genomic DNA. Translation: AAC46188.1 .
    AM406671 Genomic DNA. Translation: CAL97772.1 .
    RefSeqi YP_001032492.1. NC_009004.1.

    3D structure databases

    ProteinModelPortali O30418.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 416870.llmg_1179.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAL97772 ; CAL97772 ; llmg_1179 .
    GeneIDi 4797573.
    KEGGi llm:llmg_1179.
    PATRICi 22283506. VBILacLac4574_1210.

    Phylogenomic databases

    eggNOGi COG0076.
    HOGENOMi HOG000070228.
    KOi K01580.
    OMAi PTFQINF.
    OrthoDBi EOG6TFCPW.

    Enzyme and pathway databases

    BioCyci LLAC416870:GCDT-1204-MONOMER.

    Family and domain databases

    Gene3Di 3.40.640.10. 1 hit.
    InterProi IPR010107. Glutamate_decarboxylase.
    IPR002129. PyrdxlP-dep_de-COase.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    [Graphical view ]
    PANTHERi PTHR11999:SF1. PTHR11999:SF1. 1 hit.
    Pfami PF00282. Pyridoxal_deC. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53383. SSF53383. 1 hit.
    TIGRFAMsi TIGR01788. Glu-decarb-GAD. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.

    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: October 1, 2014
    This is version 76 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