ID A0A0H3LEP9_MYCTE Unreviewed; 460 AA.
AC A0A0H3LEP9;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 41.
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 Name=gadB {ECO:0000313|EMBL:BAL67532.1};
GN OrderedLocusNames=ERDMAN_3759 {ECO:0000313|EMBL:BAL67532.1};
OS Mycobacterium tuberculosis (strain ATCC 35801 / TMC 107 / Erdman).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=652616 {ECO:0000313|EMBL:BAL67532.1, ECO:0000313|Proteomes:UP000007568};
RN [1] {ECO:0000313|EMBL:BAL67532.1, ECO:0000313|Proteomes:UP000007568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35801 / TMC 107 / Erdman
RC {ECO:0000313|Proteomes:UP000007568};
RX PubMed=22535945; DOI=10.1128/JB.00353-12;
RA Miyoshi-Akiyama T., Matsumura K., Iwai H., Funatogawa K., Kirikae T.;
RT "Complete annotated genome sequence of Mycobacterium tuberculosis Erdman.";
RL J. Bacteriol. 194:2770-2770(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; AP012340; BAL67532.1; -; Genomic_DNA.
DR RefSeq; WP_003418277.1; NZ_KK339487.1.
DR AlphaFoldDB; A0A0H3LEP9; -.
DR SMR; A0A0H3LEP9; -.
DR KEGG; mtn:ERDMAN_3759; -.
DR PATRIC; fig|652616.3.peg.3831; -.
DR HOGENOM; CLU_019582_2_1_11; -.
DR Proteomes; UP000007568; 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 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:UP000007568}.
FT MOD_RES 277
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 460 AA; 50780 MW; B5DA3156D4C7CB4F CRC64;
MSRSHPSVPA HSIAPAYTGR MFTAPVPALR MPDESMDPEA AYRFIHDELM LDGSSRLNLA
TFVTTWMDPE AEKLMAETFD KNMIDKDEYP ATAAIEARCV SMVADLFHAE GLRDHDPTSA
TGVSTIGSSE AVMLGGLALK WRWRQRVGSW KGRMPNLVMG SNVQVVWEKF CRYFDVEPRY
LPMERGRYVI TPEQVLAAVD ENTIGVVAIL GTTYTGELEP IAEICAALDK LAAGGGVDVP
VHVDAASGGF VVPFLHPDLV WDFRLPRVVS INVSGHKYGL TYPGVGFVVW RGPEHLPEDL
VFRVNYLGGD MPTFTLNFSR PGNQVVGQYY NFLRLGRDGY TKVMQALSHT ARWLGDQLRE
VDHCEVISDG SAIPVVSFRL AGDRGYTEFD VSHELRTFGW QVPAYTMPDN ATDVAVLRIV
VREGLSADLA RALHDDAVTA LAALDKVKPG GHFDAQHFAH
//
