ID   A0A1L4BUU1_9GAMM        Unreviewed;       447 AA.
AC   A0A1L4BUU1;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   28-FEB-2018, entry version 9.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=F7310_09705 {ECO:0000313|EMBL:API87611.1};
OS   Francisella sp. TX077310.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=573570 {ECO:0000313|EMBL:API87611.1, ECO:0000313|Proteomes:UP000184222};
RN   [1] {ECO:0000313|EMBL:API87611.1, ECO:0000313|Proteomes:UP000184222}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TX077310 {ECO:0000313|EMBL:API87611.1,
RC   ECO:0000313|Proteomes:UP000184222};
RX   PubMed=27881415;
RA   Challacombe J.F., Petersen J.M., Gallegos-Graves V., Hodge D.,
RA   Pillai S., Kuske C.R.;
RT   "Whole genome relationships among Francisella bacteria of diverse
RT   origin define new species and provide specific regions for
RT   detection.";
RL   Appl. Environ. Microbiol. 0:0-0(2016).
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:RU361171};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU361171}.
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DR   EMBL; CP016796; API87611.1; -; Genomic_DNA.
DR   RefSeq; WP_072713392.1; NZ_CP016796.1.
DR   KEGG; frx:F7310_09705; -.
DR   KO; K01580; -.
DR   Proteomes; UP000184222; 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   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   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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000184222};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU361171};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU361171}.
FT   COILED      417    437       {ECO:0000256|SAM:Coils}.
FT   MOD_RES     266    266       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   447 AA;  50521 MW;  A66FDDDF3B2B1650 CRC64;
     MALHGKKNIM DDFDFFEESL PKVRIPVGSQ DPLQTYQEIK DELMLDGNSK QNLATFCQTQ
     VDDFSHKLMD DCLDKNMIDK DEYSQTAEIE SRCVNILANL WNSSAESAIG CSTTGSSEAA
     MLGGMAMKWR WRDKMKAQGK DCSKPNLVTG PVQVCWHKFA KYWDIELREI PMSKESLIMT
     PEAVIERCDE NTIGVVPTLG VTFTGQYEPV EEVCKALDKF EQETGIDIPV HVDGASGGFL
     APFIDPELKW DFRLPRVKSI NASGHKFGLS PLGVGWVIWS DKKYLPDDLV FNVNYLGGDM
     PTFALNFSRP GGQIVAQYYN FVRLGFEGYR KVHQVSYDVT KYIAGQLDDM GIFEIIHSGQ
     GGIPAVSWSL KSDKEYSLFD LSEKIRSKGW QIAAYSMPKD RQDLVVMRVL VRRGFTFDLA
     QLMIRDLKKA IQSLENKESN NRSSFSH
//