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Database: UniProt/TrEMBL
Entry: D6EAE9_9ACTN
LinkDB: D6EAE9_9ACTN
Original site: D6EAE9_9ACTN 
ID   D6EAE9_9ACTN            Unreviewed;       496 AA.
AC   D6EAE9;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   20-DEC-2017, entry version 41.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=GPA_26020 {ECO:0000313|EMBL:CBL04696.1};
OS   Gordonibacter pamelaeae 7-10-1-b.
OC   Bacteria; Actinobacteria; Coriobacteriia; Eggerthellales;
OC   Eggerthellaceae; 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-bT {ECO:0000313|EMBL:CBL04696.1};
RA   Pajon A.;
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: L-glutamate = 4-aminobutanoate + CO(2).
CC       {ECO:0000256|RuleBase:RU361171}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602129-50,
CC         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   ProteinModelPortal; D6EAE9; -.
DR   EnsemblBacteria; CBL04696; CBL04696; GPA_26020.
DR   KEGG; gpa:GPA_26020; -.
DR   PATRIC; fig|657308.3.peg.2084; -.
DR   KO; K01580; -.
DR   BioCyc; GPAM657308:G136S-1512-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; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 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_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
DR   PANTHER; PTHR43321; PTHR43321; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01788; Glu-decarb-GAD; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000008805};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU000382, ECO:0000313|EMBL:CBL04696.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008805}.
FT   MOD_RES     286    286       N6-(pyridoxal phosphate)lysine.
FT                                {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
//
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