ID   A0A1V2TH36_9NOCA        Unreviewed;       491 AA.
AC   A0A1V2TH36;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
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=B0T46_10085 {ECO:0000313|EMBL:ONM48827.1};
OS   Nocardia donostiensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=1538463 {ECO:0000313|EMBL:ONM48827.1, ECO:0000313|Proteomes:UP000188836};
RN   [1] {ECO:0000313|EMBL:ONM48827.1, ECO:0000313|Proteomes:UP000188836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=X1655 {ECO:0000313|EMBL:ONM48827.1,
RC   ECO:0000313|Proteomes:UP000188836};
RX   PubMed=26914251; DOI=10.1007/s10482-016-0667-8;
RA   Ercibengoa M., Bell M., Marimon J.M., Humrighouse B., Klenk H.P.,
RA   Potter G., Perez-Trallero E.;
RT   "Nocardia donostiensis sp. nov., isolated from human respiratory
RT   specimens.";
RL   Antonie Van Leeuwenhoek 109:653-660(2016).
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:ONM48827.1}.
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DR   EMBL; MUMY01000007; ONM48827.1; -; Genomic_DNA.
DR   RefSeq; WP_077116307.1; NZ_MUMY01000007.1.
DR   AlphaFoldDB; A0A1V2TH36; -.
DR   STRING; 1538463.B0T36_21870; -.
DR   OrthoDB; 3401800at2; -.
DR   Proteomes; UP000188836; Unassembled WGS sequence.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000188836}.
FT   REGION          450..491
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         279
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   491 AA;  54433 MW;  A4F8ABDD33BE9591 CRC64;
     MALTHPSHPG EHRRRADIHV NPVFTREPVE VPRNRLPAGG LDSDTAYQVV HDELLLDGNA
     RLNLATFVTT WMEPTAHTLM GECFDKNMID KDEYPRTADL EQRCVRMLAD LWHAVDPDNT
     IGCSTTGSSE ACMLAGLALK RRWQHRRRAA GQQADRPNLV MGSNVQVCWE KFADYWDVEP
     RLVPMSGTRF HLTAEEAVAR CDENTVGVVA ILGSTFDGSY EPVAQICAAL DRVQAEQGWD
     IPVHVDGASG AMFAPFCDPD LEWDFRLPRV ASINTSGHKY GLVYPGVGWV LWRDPEALPD
     DLVFRVNYLG GQMPTFALNF SRPGAQVVAQ YYMFLRLGRS GYRRIQQYCR EVAADLADRI
     ARMGPFELIT DGRQLPVFAF TLAPGETGYS VFDVSAALRE QGWLVPAYAF PADREDLAVL
     RIVVRNGFSH DLADLLIEAI ERALPRLRAQ RGPARGPETA SFSHGADAYP SGAGAAEGRS
     VPAHAKETLS R
//