ID A0A2Z3YY12_9CORY Unreviewed; 466 AA.
AC A0A2Z3YY12;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
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:AWT27434.1};
GN ORFNames=Csp1_26910 {ECO:0000313|EMBL:AWT27434.1};
OS Corynebacterium provencense.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1737425 {ECO:0000313|EMBL:AWT27434.1, ECO:0000313|Proteomes:UP000247696};
RN [1] {ECO:0000313|Proteomes:UP000247696}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17KM38 {ECO:0000313|Proteomes:UP000247696};
RA Kittl S., Brodard I., Rychener L., Jores J., Roosje P., Gobeli Brawand S.;
RT "Otitis media/interna in a cat caused by the recently described species
RT Corynebacterium provencense.";
RL Submitted (NOV-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; CP024988; AWT27434.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z3YY12; -.
DR STRING; 1737425.GCA_900049755_01718; -.
DR KEGG; cpre:Csp1_26910; -.
DR OrthoDB; 3401800at2; -.
DR Proteomes; UP000247696; 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:UP000247696}.
FT MOD_RES 267
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 466 AA; 52709 MW; 103AE0BA3AE1007B CRC64;
MSDLELNPLF ARADEVTSFP RHRIPEVGSL PETAYQLIHD EAMLDGNARM NLATFVGTWM
DDYADRLYSE AFDKNMIDKD EYPATAEIED RCWRMIARLW NAPDPDHTLG TSTVGSSEAC
MLGGLALKRR WQHGRRETGK STERPNIVLS SAVQVCWEKF CNYFEVEPRY VPVSEEHRVL
DGHDLDSYVD ENTIGVVVIM GVTYTGMYEP VAEIAEALDE IQSRRGLDIR IHVDAASGGM
IAPFLQPDLE WDFRLPRVAS INTSGHKYGL VYPGLGWIVW RTREDLPEDL IFRVSYLGGD
MPTLALNFSR PGAQVLLQYY LFLQLGMDGY RRVQGATMDV ARYLAGEIGK MPDFELWSDD
PDIPVFAWRL VGEDARTGGG VRRGRKWTLY DLSDRLRMHG WQVPAYPMPD NLSDMTVQRI
VVRNGMSHDL ATLFVRDLRT CVHYLDGLDA PLPSSAVGGH GTGFHH
//
