ID   K0EH34_NOCB7            Unreviewed;       467 AA.
AC   K0EH34;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 58.
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=O3I_003125 {ECO:0000313|EMBL:AFT98587.1};
OS   Nocardia brasiliensis (strain ATCC 700358 / HUJEG-1).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=1133849 {ECO:0000313|EMBL:AFT98587.1, ECO:0000313|Proteomes:UP000006304};
RN   [1] {ECO:0000313|EMBL:AFT98587.1, ECO:0000313|Proteomes:UP000006304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700358 {ECO:0000313|Proteomes:UP000006304};
RX   PubMed=22535940; DOI=10.1128/JB.00210-12;
RA   Vera-Cabrera L., Ortiz-Lopez R., Elizondo-Gonzalez R., Perez-Maya A.A.,
RA   Ocampo-Candiani J.;
RT   "Complete genome sequence of Nocardia brasiliensis HUJEG-1.";
RL   J. Bacteriol. 194:2761-2762(2012).
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}.
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DR   EMBL; CP003876; AFT98587.1; -; Genomic_DNA.
DR   RefSeq; WP_014981448.1; NC_018681.1.
DR   AlphaFoldDB; K0EH34; -.
DR   STRING; 1133849.O3I_003125; -.
DR   KEGG; nbr:O3I_003125; -.
DR   eggNOG; COG0076; Bacteria.
DR   HOGENOM; CLU_019582_2_1_11; -.
DR   Proteomes; UP000006304; Chromosome.
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   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:UP000006304}.
FT   REGION          443..467
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         262
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   467 AA;  51645 MW;  9744C34C4B07D8F7 CRC64;
     MSETPDSDDL FALPGINRIA PRGGFPQHEL LPQVAYEIVH DELLLDGVSR MNLATFCTTW
     SDDTARRLMA ESLDKNIVDK DEYPQTAELE RRCVRMIADL WHCPDPAGTH GTSTTGSSEA
     AMLGGLAAKF RWRQRGGTGT PNFVCGPVQV CWEKFARYFD VEIRQVPLSG DRLTLHPDEV
     AAHCDERTIM VVPTFGQTFT GLYEDVAGIS RALDRVQEVS GLDIPIHVDA ASGGFLAPFT
     APDLVWDFRL PRVKSINASG HKTGLAPLGA GWAIWREAAD LPAELIFDVD YLGGSVGTFN
     LNFSRPGGQA ITQYYEFIRL GRIGYTRVQS ASYRAARKLA AGLREFGIFE PIHDGDPRHG
     ITAVSWRLTG DPGFNLYDLS DRLRSRGWLI AAYPLPAHRE NEIIMRAVIR HGFTVDMADL
     LLADFDRCVK QLARHPFSTS LTRQEAGGFT HSATAQVPDP KRDTHPA
//