ID D6EAE9_9ACTN Unreviewed; 496 AA.
AC D6EAE9;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 24-JAN-2024, entry version 69.
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=GPA_26020 {ECO:0000313|EMBL:CBL04696.1};
OS Gordonibacter pamelaeae 7-10-1-b.
OC Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC Gordonibacter.
OX NCBI_TaxID=657308 {ECO:0000313|EMBL:CBL04696.1, ECO:0000313|Proteomes:UP000008805};
RN [1] {ECO:0000313|EMBL:CBL04696.1, ECO:0000313|Proteomes:UP000008805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7-10-1-b {ECO:0000313|Proteomes:UP000008805};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Timmis K., Oxley A., Wurdemann D.;
RT "The genome sequence of Gordonibacter pamelaeae 7-10-1-bT.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL04696.1, ECO:0000313|Proteomes:UP000008805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7-10-1-b {ECO:0000313|Proteomes:UP000008805};
RA Pajon A.;
RL Submitted (MAR-2010) 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; FP929047; CBL04696.1; -; Genomic_DNA.
DR RefSeq; WP_015540040.1; NC_021021.1.
DR AlphaFoldDB; D6EAE9; -.
DR GeneID; 78358449; -.
DR KEGG; gpa:GPA_26020; -.
DR PATRIC; fig|657308.3.peg.2084; -.
DR HOGENOM; CLU_019582_2_2_11; -.
DR BioCyc; GPAM657308:GPA_RS12120-MONOMER; -.
DR Proteomes; UP000008805; 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:UP000008805}.
FT REGION 473..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 286
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 496 AA; 56136 MW; 35B604661D7FDEBE CRC64;
MKEQTSTSKI LDSMDEGTKY STPIFGSEAS DVAMPRLKMN DQPVEPRIAY EMIKEYLSIE
GNATQNLTTF CQTYMEPMAT KIMAETMEKN AIDKDEYPMT ADLENRCVAM IGDLWHADPA
EEPMGTSTVG SSEACMLGGL GMLFRWKKLA KDAGIDIYTE QRPNLVISAG YQVCWEKFCR
YWDIEMRLVP LEKDHLSLNM DTVMDYVDDH TIGITAILGI TYTGKFDDVQ KLDELVEAYN
QEHPKLPIRI HVDGASGGMF APFVEPDLVW DFQLKNVWSI NCSGHKYGLV YPGIGWVVWR
SKEALPEDLI FWVSYLGGEE ATMAINFSRS ASQIVGQYYV LMRNGFEGFK EIQERTLDVA
RYLAAELKEM GIFEIYEDAS HIPIVCWGLK DDADVEWSLY DLSDRLRMSG WLVPAYPMPA
DMQDTTVQRV VARADFSMQL CIKLVEDMKK EMDTLNKAKF VTGNTQGVIQ TGFNHGGRSA
VDKGEKVQTK AKTTQK
//