ID B1MG69_MYCA9 Unreviewed; 476 AA.
AC B1MG69;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 91.
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=MAB_3740c {ECO:0000313|EMBL:CAM63814.1};
OS Mycobacteroides abscessus (strain ATCC 19977 / DSM 44196 / CCUG 20993 / CIP
OS 104536 / JCM 13569 / NCTC 13031 / TMC 1543 / L948) (Mycobacterium
OS abscessus).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacteroides; Mycobacteroides abscessus.
OX NCBI_TaxID=561007 {ECO:0000313|EMBL:CAM63814.1, ECO:0000313|Proteomes:UP000007137};
RN [1] {ECO:0000313|EMBL:CAM63814.1, ECO:0000313|Proteomes:UP000007137}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19977 / DSM 44196 / CIP 104536 / JCM 13569 / NCTC 13031 /
RC TMC 1543 {ECO:0000313|Proteomes:UP000007137};
RX PubMed=19543527; DOI=10.1371/journal.pone.0005660;
RA Ripoll F., Pasek S., Schenowitz C., Dossat C., Barbe V., Rottman M.,
RA Macheras E., Heym B., Herrmann J.L., Daffe M., Brosch R., Risler J.L.,
RA Gaillard J.L.;
RT "Non mycobacterial virulence genes in the genome of the emerging pathogen
RT Mycobacterium abscessus.";
RL PLoS ONE 4:E5660-E5660(2009).
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; CU458896; CAM63814.1; -; Genomic_DNA.
DR RefSeq; WP_005123053.1; NZ_MLCG01000001.1.
DR AlphaFoldDB; B1MG69; -.
DR GeneID; 66969167; -.
DR KEGG; mab:MAB_3740c; -.
DR Proteomes; UP000007137; 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}.
FT MOD_RES 292
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 476 AA; 52637 MW; B47A2333D52408D8 CRC64;
MSKSRDQFRL SAHAGKINAS AFSPAYTGRL STAPVPALRL PDEPMDPQAA YRFIHDELML
DGSSRLNLAT FVTTWMDPEA EKLMAETFDK NMIDKDEYPA TAAIESRCVA MVADLFHADN
LSTEDPSSAV GVSTIGSSEA VMLAGLALKW RWRTKIGGTD GTGWKGRTPN LVMGSNVQVV
WEKFCRYFDV EPRYLPMAKG RYVITPEQVL EVVDEDTIGV VGILGTTFTG ELEPIAAICA
ALDKLAATPG KPDVPVHVDA ASGGFVVPFL HPELHWDFRL PRVVSINVSG HKYGLTYPGI
GFVVWRGKEH LPEDLVFRVN YLGGDMPTFT LNFSRPGNQV VGQYYNFLRL GRAGYAQVMR
CLSETARWFG DELGKSEHFE VITDGSAIPV VSFRLKGKRP YTEFDISHSL RAFGWQVPAY
TMPDDVTDIA VLRVVVREGF SGDLARALRD DLNTVLKGLD ELKPNGHFDE VQPFAH
//