ID   I4BF37_MYCCN            Unreviewed;       467 AA.
AC   I4BF37;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 65.
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};
DE   Flags: Precursor;
GN   OrderedLocusNames=Mycch_1085 {ECO:0000313|EMBL:AFM15894.1};
OS   Mycolicibacterium chubuense (strain NBB4) (Mycobacterium chubuense).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=710421 {ECO:0000313|EMBL:AFM15894.1, ECO:0000313|Proteomes:UP000006057};
RN   [1] {ECO:0000313|EMBL:AFM15894.1, ECO:0000313|Proteomes:UP000006057}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBB4 {ECO:0000313|EMBL:AFM15894.1,
RC   ECO:0000313|Proteomes:UP000006057};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Mattes T.,
RA   Holmes A., Rutledge P., Paulsen I., Coleman N., Woyke T.;
RT   "Complete sequence of chromosome of Mycobacterium chubuense NBB4.";
RL   Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
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; CP003053; AFM15894.1; -; Genomic_DNA.
DR   RefSeq; WP_014814378.1; NC_018027.1.
DR   AlphaFoldDB; I4BF37; -.
DR   STRING; 710421.Mycch_1085; -.
DR   KEGG; mcb:Mycch_1085; -.
DR   PATRIC; fig|710421.3.peg.1094; -.
DR   eggNOG; COG0076; Bacteria.
DR   HOGENOM; CLU_019582_2_2_11; -.
DR   OrthoDB; 3401800at2; -.
DR   Proteomes; UP000006057; 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:UP000006057}.
FT   MOD_RES         278
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   467 AA;  51782 MW;  F38F4DFE3138ADDB CRC64;
     MPNVSRHTSL TPAYTGRMFT SPIPALRLPD ESMDPEQAYR FIHDELMLDG SSRLNLATFV
     TTWMDPEAGQ LMSETFDKNM IDKDEYPVTA AIEQRCVCMV ADLFHAEHLR DDDPSTAIGV
     STIGSSEAVM LAGLALKWRW RQKLEAAGQD WKGRTPNLVM GSNVQVVWEK FCRYFDVEAR
     YLPMDKGRYV ITPEQVVDAV DEDTIGVVAI LGTTFTGELE PVGEICAALD TLARGDGPDV
     PVHVDAASGG FVVPFLHPDM VWDFRLPRVV SINVSGHKYG LTYPGIGFVV WRNADHLPEE
     LVFRVNYLGG DMPTFTLNFS RPGNQVVGQY YNFLRLGRDG YMSVMHCLSD TAQWLARELA
     GMSGPDNTPV FDVISDGSAI PVVAFKLVEG TKFTVFDVSA LLRSYGWQVP AYTMPDHASD
     IAVLRIVVRE GFSANLARAL RDDLVEVLGK LERTGVAGFS DEEHFAH
//