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Database: UniProt/TrEMBL
Entry: Q1MRQ9_LAWIP
LinkDB: Q1MRQ9_LAWIP
Original site: Q1MRQ9_LAWIP 
ID   Q1MRQ9_LAWIP            Unreviewed;       502 AA.
AC   Q1MRQ9;
DT   30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   30-MAY-2006, sequence version 1.
DT   25-OCT-2017, entry version 76.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   Name=gad {ECO:0000313|EMBL:CAJ54317.1};
GN   OrderedLocusNames=LI0261 {ECO:0000313|EMBL:CAJ54317.1};
OS   Lawsonia intracellularis (strain PHE/MN1-00).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Lawsonia.
OX   NCBI_TaxID=363253 {ECO:0000313|EMBL:CAJ54317.1, ECO:0000313|Proteomes:UP000002430};
RN   [1] {ECO:0000313|EMBL:CAJ54317.1, ECO:0000313|Proteomes:UP000002430}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHE/MN1-00 {ECO:0000313|EMBL:CAJ54317.1,
RC   ECO:0000313|Proteomes:UP000002430};
RA   Kaur K., Zhang Q., Beckler D., Munir S., Li L., Kinsley K., Herron L.,
RA   Peterson A., May B., Singh S., Gebhart C., Kapur V.;
RT   "The complete genome sequence of Lawsonia intracellularis: the
RT   causative agent of proliferative enteropathy.";
RL   Submitted (NOV-2005) 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:RU361171};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU361171}.
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DR   EMBL; AM180252; CAJ54317.1; -; Genomic_DNA.
DR   RefSeq; WP_011526343.1; NC_008011.1.
DR   ProteinModelPortal; Q1MRQ9; -.
DR   STRING; 363253.LI0261; -.
DR   KEGG; lip:LI0261; -.
DR   eggNOG; ENOG4105CVK; Bacteria.
DR   eggNOG; COG0076; LUCA.
DR   HOGENOM; HOG000070228; -.
DR   KO; K01580; -.
DR   OMA; RPNLVMG; -.
DR   Proteomes; UP000002430; 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:UP000002430};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002430}.
FT   MOD_RES     302    302       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   502 AA;  57125 MW;  360AB851B33722E6 CRC64;
     MATARKAVVK KMPVGHGTKR GSMGNRTQKS SMSNGVVRHE LLDDVFAEDD LSQTLPKYQM
     PLYEHRPRDI YQAVHDELML DGNARQNLAT FCQTWVDPEI HKLMDECVAK NMIDKDEYPQ
     TAELEMRCVN MLADLWNSPD PTNTIGCSAI GSSEAAMLGG MALKWRWRAQ RKKAGKSTDK
     PNLVCGPVQI CWHKFARYWD IELREIPMEK NRLIMSPEEA IKRCDENTIG VVPTLGVTYT
     GQYEPVEEVS NALDALQKKK GWDIPIHVDA ASGGFLAPFI EPELVWDFRL PRVKSINSSG
     HKFGLAPLGM GWVVWREKTD LPEDLIFWVN YLGSNIPTFA INFSRPGGQI VCQYYNLLRL
     GREGYRRIHQ ACYDTTDYLA NELTKTGIFK ILYGGKTGIP ALTWTLKDEK KYPFSLYDLS
     DRLRTRGWQV PAYSMPANRT DLVVMRVLVR HGFDHDLADL LVNDIHRAIE HLKQNPRRKP
     LGSGQVTSYD HSGRSSIPQK KK
//
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