GenomeNet

Database: UniProt/TrEMBL
Entry: T2F5M9_LACLC
LinkDB: T2F5M9_LACLC
Original site: T2F5M9_LACLC 
ID   T2F5M9_LACLC            Unreviewed;       466 AA.
AC   T2F5M9;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|ARBA:ARBA00012421, ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|ARBA:ARBA00012421, ECO:0000256|RuleBase:RU361171};
GN   ORFNames=kw2_1250 {ECO:0000313|EMBL:AGV73208.1};
OS   Lactococcus cremoris subsp. cremoris KW2.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus; Lactococcus cremoris subsp. cremoris.
OX   NCBI_TaxID=1295826 {ECO:0000313|EMBL:AGV73208.1, ECO:0000313|Proteomes:UP000016704};
RN   [1] {ECO:0000313|EMBL:AGV73208.1, ECO:0000313|Proteomes:UP000016704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KW2 {ECO:0000313|EMBL:AGV73208.1};
RX   PubMed=24009606; DOI=10.3389/fmicb.2013.00257;
RA   Kelly W.J., Altermann E., Lambie S.C., Leahy S.C.;
RT   "Interaction between the genomes of Lactococcus lactis and phages of the
RT   P335 species.";
RL   Front. Microbiol. 4:257-257(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-glutamate = 4-aminobutanoate + CO2;
CC         Xref=Rhea:RHEA:17785, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:59888; EC=4.1.1.15;
CC         Evidence={ECO:0000256|ARBA:ARBA00000018,
CC         ECO:0000256|RuleBase:RU361171};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU000382}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP004884; AGV73208.1; -; Genomic_DNA.
DR   RefSeq; WP_021037313.1; NC_022369.1.
DR   AlphaFoldDB; T2F5M9; -.
DR   GeneID; 61109545; -.
DR   KEGG; llw:kw2_1250; -.
DR   PATRIC; fig|1295826.3.peg.1246; -.
DR   HOGENOM; CLU_019582_2_1_9; -.
DR   Proteomes; UP000016704; Chromosome.
DR   GO; GO:0004058; F:aromatic-L-amino-acid decarboxylase activity; IEA:UniProt.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006536; P:glutamate metabolic process; IEA:InterPro.
DR   CDD; cd06450; DOPA_deC_like; 1.
DR   Gene3D; 3.90.1150.160; -; 1.
DR   Gene3D; 4.10.280.50; -; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR010107; Glutamate_decarboxylase.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   NCBIfam; TIGR01788; Glu-decarb-GAD; 1.
DR   PANTHER; PTHR43321; GLUTAMATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43321:SF3; GLUTAMATE DECARBOXYLASE; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382}.
FT   MOD_RES         277
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   466 AA;  53897 MW;  5F544713941DCBEA CRC64;
     MLYGKENRDE AEFLEPIFGS ESEQVDLPKY KLAQQSIEPR VAYQLVQDEM LDEGNARLNL
     ATFCQTYMEP EAVKLMSQTL EKNAIDKSEY PRTTEIENRC VNMIADLWNA SEKEKFMGTS
     TIGSSEACML GGMAMKFSWR KRAEKLGLDI NAKKPNLVIS SGYQVCWEKF CVYWDIEMRE
     VPMDREHMSI NLEKVMDYVD EYTIGVVGIM GITYTGRYDD IKALDNLIEE YNKQTDYKVY
     IHVDAASGGL YAPFVEPELE WDFRLKNVIS INTSGHKYGL VYPGVGWVLW RDKKYLPEEL
     IFKVSYLGGE LPTMAINFSH SASQLIGQYY NFVRYGFDGY KAIHERTHKV AMYLAEEIEK
     TGMFEIMNDG SQLPIVCYKL KENSNLGWNL YDLADRLLMK GWQVPAYPLP KNLENEIIQR
     LVIRADFGMN MAFNYVQDMQ EAIDALNKAH ILFHQEPENK TYGFTH
//
DBGET integrated database retrieval system