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Database: UniProt
Entry: A0A0R1WC67_9LACO
LinkDB: A0A0R1WC67_9LACO
Original site: A0A0R1WC67_9LACO 
ID   A0A0R1WC67_9LACO        Unreviewed;       466 AA.
AC   A0A0R1WC67;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 43.
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=FD16_GL001257 {ECO:0000313|EMBL:KRM13113.1};
OS   Paucilactobacillus suebicus DSM 5007 = KCTC 3549.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Paucilactobacillus.
OX   NCBI_TaxID=1423807 {ECO:0000313|EMBL:KRM13113.1, ECO:0000313|Proteomes:UP000051820};
RN   [1] {ECO:0000313|EMBL:KRM13113.1, ECO:0000313|Proteomes:UP000051820}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5007 {ECO:0000313|EMBL:KRM13113.1,
RC   ECO:0000313|Proteomes:UP000051820};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRM13113.1}.
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DR   EMBL; AZGF01000003; KRM13113.1; -; Genomic_DNA.
DR   RefSeq; WP_010622133.1; NZ_BACO01000042.1.
DR   AlphaFoldDB; A0A0R1WC67; -.
DR   STRING; 1423807.FD16_GL001257; -.
DR   PATRIC; fig|1423807.3.peg.1283; -.
DR   eggNOG; COG0076; Bacteria.
DR   OrthoDB; 9803665at2; -.
DR   Proteomes; UP000051820; Unassembled WGS sequence.
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   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         277
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   466 AA;  53647 MW;  DBD0DD6EA186753E CRC64;
     MLYGKHDQEE NSLLRPTFGS NGEDHDLPKY RLNKESLSPR IAYQLVKDQL LDEGNSRLNL
     ATFCQTFMEP EAVKLMSESL EKNAIDKSEY PRTAEIENRC VSIIANLWNA DKKEKYMGTS
     TVGSSEACML GGMAMKFSWR KRAEKLGLDI NAHKPNLVIS SGYQVCWEKF CTYWDIEMRT
     VPLDQNHQSL NMDTVMDYVD KYTIGIVGIL GITYTGRYDD IQKLDQLVED YNAHTEYKVY
     IHVDAASGGF YTPFMEPNLK WDFRLKNVVS INTSGHKYGL VYPGIGWILW RDAKFVPKKL
     IFKVSYLGGE MPTMAINFSH SAAQLIGQYY NFIRFGSDGY YDIQKHTHDV AAYIAKEIKK
     MDIFDVINDG AQLPIICYKL TKDDNREWTL YDLADRLLMK GWQVPAYPLP KDLDKVVIQR
     IVVRSDLGMN MAHNYVQDLK QAVKDLNNAH VLFHEKAEIK TYGFTH
//
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