ID A0A1W1WF42_SULTA Unreviewed; 466 AA.
AC A0A1W1WF42;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=SAMN00768000_1836 {ECO:0000313|EMBL:SMC04789.1};
OS Sulfobacillus thermosulfidooxidans (strain DSM 9293 / VKM B-1269 / AT-1).
OC Bacteria; Bacillota; Clostridia; Eubacteriales;
OC Clostridiales Family XVII. Incertae Sedis; Sulfobacillus.
OX NCBI_TaxID=929705 {ECO:0000313|EMBL:SMC04789.1, ECO:0000313|Proteomes:UP000192660};
RN [1] {ECO:0000313|Proteomes:UP000192660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9293 {ECO:0000313|Proteomes:UP000192660};
RA Varghese N., Submissions S.;
RL Submitted (APR-2017) 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; FWWY01000001; SMC04789.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W1WF42; -.
DR STRING; 28034.BFX07_01860; -.
DR Proteomes; UP000192660; Unassembled WGS sequence.
DR GO; GO:0004058; F:aromatic-L-amino-acid decarboxylase activity; IEA:UniProt.
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:UP000192660}.
FT MOD_RES 278
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 466 AA; 52770 MW; C83C0B623E9DC8AF CRC64;
MSWRPDRHMK KASEEVAINP LFARRGEESV PRYRLSEEGL LPETAYQIVH DELTLDGSAR
LNLATFVGTW MEPEAQKLYV EAANKNIIDK DEYPETAAIE ERCLKILANL WNAPDPANSI
GVSTTGSSEA CMLGGLALKR RWQLSRRQQG KSTDHPNIVF SSAVQVVWEK FANYFEVEPR
YVNITPEHPY LTPEGVIKAV DENTIGVVPI LGVTYTGSYE PVEAIAQALD DLEKRTGLSI
PIHVDAASGG FVAPFLQPDL VWDFRLPRVH SINTSGHKYG LVYPGLGWVL WRDKTLLPEE
LIFNVSYLGG SMPTFGLNFS RPGAQVLLQY YNFLRLGRQG YYTVQKTCQN VAHFLAQEIG
AMEPFELVTD GSDLPVFAWR KRPEENPLWS LEDLSFVLRE RGWQVPAYPL PPTMQDVTIM
RIVVRNSFSM DMAQLFLDDL NRAVAYLQGL DHPFPQALRQ HKPFHH
//
