ID   E6TDE0_MYCSR            Unreviewed;       468 AA.
AC   E6TDE0;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 73.
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   OrderedLocusNames=Mspyr1_43520 {ECO:0000313|EMBL:ADU00909.1};
OS   Mycolicibacterium gilvum (strain DSM 45189 / LMG 24558 / Spyr1)
OS   (Mycobacterium gilvum).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=278137 {ECO:0000313|EMBL:ADU00909.1, ECO:0000313|Proteomes:UP000008916};
RN   [1] {ECO:0000313|Proteomes:UP000008916}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45189 / LMG 24558 / Spyr1
RC   {ECO:0000313|Proteomes:UP000008916};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., LaButti K., Ivanova N.M., Mikhailova N.M., Land M., Hauser L.,
RA   Koukkou A.I., Drainas C., Kyrpides N., Woyke T.;
RT   "Complete sequence of chromosome of Mycobacterium sp. Spyr1.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADU00909.1, ECO:0000313|Proteomes:UP000008916}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45189 / LMG 24558 / Spyr1
RC   {ECO:0000313|Proteomes:UP000008916};
RX   PubMed=22180818;
RA   Kallimanis A., Karabika E., Mavromatis K., Lapidus A., Labutti K.M.,
RA   Liolios K., Ivanova N., Goodwin L., Woyke T., Velentzas A.D.,
RA   Perisynakis A., Ouzounis C.C., Kyrpides N.C., Koukkou A.I., Drainas C.;
RT   "Complete genome sequence of Mycobacterium sp. strain (Spyr1) and
RT   reclassification to Mycobacterium gilvum Spyr1.";
RL   Stand. Genomic Sci. 5:144-153(2011).
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; CP002385; ADU00909.1; -; Genomic_DNA.
DR   RefSeq; WP_011895765.1; NC_014814.1.
DR   AlphaFoldDB; E6TDE0; -.
DR   KEGG; msp:Mspyr1_43520; -.
DR   HOGENOM; CLU_019582_2_1_11; -.
DR   Proteomes; UP000008916; 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}.
FT   MOD_RES         279
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   468 AA;  51707 MW;  F8B73400E0062D48 CRC64;
     MPNVSRHSSL APAYTGRMSM SPVPALRLPD ESMEPEQAYR FIHDELMLDG SSRLNLATFV
     TTWMDPEAGQ LMSETFDKNM IDKDEYPVTA AIEQRCVCMV ADLFHAENLR DDDPSTAIGV
     STVGSSEAVM LAGLAMKWRW RDKFAGKDGD GWKGRTPNLV MGSNVQVVWE KFCRYFDVEA
     RYLPMEKGRY VITPEQVLDA VDEDTIGVVA ILGTTFTGEL EPVAEICAAL DALAAGGGCD
     VPVHVDAASG GFVVPFLNPL LVWDFRLPRV VSINVSGHKY GLTYPGIGFV VWRNAEHLPE
     DLVFRVNYLG GDMPTFTLNF SRPGNQVVGQ YYNFLRLGRD GYTQVMHALA DTAQWLAREL
     EGMTGSDHKP VFEVITDGSA IPVVAFRLTE GAKFTVFDIS ALLRSYGWQV PAYTMPEDAT
     DIAVLRIVVR EGFSANLARA LRDDLREVLG KLDKVGIGGF SDEEHFAH
//