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Database: UniProt/TrEMBL
Entry: Q5NEB8_FRATT A0A0G2RPH9_FRATT
LinkDB: Q5NEB8_FRATT A0A0G2RPH9_FRATT
Original site: Q5NEB8_FRATT A0A0G2RPH9_FRATT 
ID   Q5NEB8_FRATT            Unreviewed;       448 AA.
AC   Q5NEB8;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   25-OCT-2017, entry version 90.
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:CAG46355.1};
GN   OrderedLocusNames=FTT_1722c {ECO:0000313|EMBL:CAG46355.1};
OS   Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=177416 {ECO:0000313|EMBL:CAG46355.1, ECO:0000313|Proteomes:UP000001174};
RN   [1] {ECO:0000313|EMBL:CAG46355.1, ECO:0000313|Proteomes:UP000001174}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCHU S4 / Schu 4 {ECO:0000313|Proteomes:UP000001174};
RX   PubMed=15640799; DOI=10.1038/ng1499;
RA   Larsson P., Oyston P.C.F., Chain P., Chu M., Duffield M.,
RA   Fuxelius H.H., Garcia E., Halltorp G., Johansson D., Isherwood K.,
RA   Karp P., Larsson E., Lui Y., Michell S., Prior J., Prior R.,
RA   Sjostedt A., Svensson K., Thompson N., Vergez L., Wagg J., Wren B.,
RA   Lindler L.E., Andersson S.G., Forsman M., Titball R.W.;
RT   "The complete genome sequence of Francisella tularensis, the causative
RT   agent of tularemia.";
RL   Nat. Genet. 37:153-159(2005).
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; AJ749949; CAG46355.1; -; Genomic_DNA.
DR   RefSeq; WP_003022692.1; NZ_CP010290.1.
DR   RefSeq; YP_170624.1; NC_006570.2.
DR   IntAct; Q5NEB8; 1.
DR   STRING; 177416.FTT_1722c; -.
DR   DNASU; 3191876; -.
DR   EnsemblBacteria; AJI68933; AJI68933; BZ14_995.
DR   EnsemblBacteria; CAG46355; CAG46355; FTT_1722c.
DR   GeneID; 3191876; -.
DR   KEGG; ftu:FTT_1722c; -.
DR   PATRIC; fig|177416.36.peg.1003; -.
DR   eggNOG; ENOG4105CVK; Bacteria.
DR   eggNOG; COG0076; LUCA.
DR   HOGENOM; HOG000070228; -.
DR   KO; K01580; -.
DR   OMA; DSCGCVT; -.
DR   Proteomes; UP000001174; 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:UP000001174};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU361171, ECO:0000313|EMBL:CAG46355.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU361171};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001174}.
FT   MOD_RES     266    266       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   448 AA;  50815 MW;  2A48F8FD23CA64D4 CRC64;
     MALHGKKDTI DNLDFFEQSL PKFKLPLNSQ DPLEVYQEIK DELMLDGNSK QNLATFCQTE
     VDDFIHKLMD DCIDKNMIDK DEYPQTAEIE SRCVNILANL WNSSAENAIG CSTTGSSEAA
     MLGGMAMKWR WRDKMKAQGK DYTKPNLVTG PVQVCWHKFA RYWDIELREI PMSNESLIMT
     PEAVLERCDE NTIGVVPTLG VTFTGQYEPV EQVCKALDDF ERQTGVDIPV HVDAASGGFL
     APFVEPELKW DFRLPRVKSI NSSGHKFGLS PLGVGWVIWA DKKYLPDDLI FNVNYLGGNM
     PAFALNFSRL GGQIVAQYYN FVRLGFEGYK KVHQLCYDVA EYIAKELRKM EIFEIIHAGE
     GGIPAVSWSL KATKEYSLFD ISEKVRAKGW QIAAYTMPNN REDLVVMRVL VRRGFSYDLA
     QLMIRDLVAV IDSLEGKLKI LKRSSFAH
//
  All links  
Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (3)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (2)   
   RefSeq(pep) (2)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (6)   
   InterPro (5)   
   Pfam (1)   
Literature (1)   
   PubMed (1)   
All databases (17)   

Download RDF
ID   A0A0G2RPH9_FRATT        Unreviewed;       448 AA.
AC   A0A0G2RPH9;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   25-OCT-2017, entry version 4.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=BZ14_995 {ECO:0000313|EMBL:AJI68933.1};
OS   Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=177416 {ECO:0000313|EMBL:AJI68933.1, ECO:0000313|Proteomes:UP000031862};
RN   [1] {ECO:0000313|EMBL:AJI68933.1, ECO:0000313|Proteomes:UP000031862}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCHU S4 {ECO:0000313|Proteomes:UP000031862};
RX   PubMed=25931589;
RA   Johnson S.L., Daligault H.E., Davenport K.W., Coyne S.R., Frey K.G.,
RA   Koroleva G.I., Broomall S.M., Bishop-Lilly K.A., Bruce D.C.,
RA   Chertkov O., Freitas T., Jaissle J., Ladner J.T., Rosenzweig C.N.,
RA   Gibbons H.S., Palacios G.F., Redden C.L., Xu Y., Minogue T.D.,
RA   Chain P.S.;
RT   "Genome sequencing of 18 francisella strains to aid in assay
RT   development and testing.";
RL   Genome Announc. 3:0-0(2015).
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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP010290; AJI68933.1; -; Genomic_DNA.
DR   RefSeq; WP_003022692.1; NZ_CP010290.1.
DR   RefSeq; YP_170624.1; NC_006570.2.
DR   GeneID; 3191876; -.
DR   KEGG; ftu:FTT_1722c; -.
DR   eggNOG; ENOG4105CVK; Bacteria.
DR   eggNOG; COG0076; LUCA.
DR   KO; K01580; -.
DR   Proteomes; UP000031862; 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:UP000031862};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU361171, ECO:0000313|EMBL:AJI68933.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU361171}.
FT   MOD_RES     266    266       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   448 AA;  50815 MW;  2A48F8FD23CA64D4 CRC64;
     MALHGKKDTI DNLDFFEQSL PKFKLPLNSQ DPLEVYQEIK DELMLDGNSK QNLATFCQTE
     VDDFIHKLMD DCIDKNMIDK DEYPQTAEIE SRCVNILANL WNSSAENAIG CSTTGSSEAA
     MLGGMAMKWR WRDKMKAQGK DYTKPNLVTG PVQVCWHKFA RYWDIELREI PMSNESLIMT
     PEAVLERCDE NTIGVVPTLG VTFTGQYEPV EQVCKALDDF ERQTGVDIPV HVDAASGGFL
     APFVEPELKW DFRLPRVKSI NSSGHKFGLS PLGVGWVIWA DKKYLPDDLI FNVNYLGGNM
     PAFALNFSRL GGQIVAQYYN FVRLGFEGYK KVHQLCYDVA EYIAKELRKM EIFEIIHAGE
     GGIPAVSWSL KATKEYSLFD ISEKVRAKGW QIAAYTMPNN REDLVVMRVL VRRGFSYDLA
     QLMIRDLVAV IDSLEGKLKI LKRSSFAH
//
  All links  
Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (3)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (2)   
   RefSeq(pep) (2)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (6)   
   InterPro (5)   
   Pfam (1)   
Literature (1)   
   PubMed (1)   
All databases (17)   

Download RDF
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