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Database: UniProt/TrEMBL
Entry: A0A0K1Q1K5_9DELT
LinkDB: A0A0K1Q1K5_9DELT
Original site: A0A0K1Q1K5_9DELT 
ID   A0A0K1Q1K5_9DELT        Unreviewed;       464 AA.
AC   A0A0K1Q1K5;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   05-JUL-2017, entry version 14.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=AKJ09_05943 {ECO:0000313|EMBL:AKU99279.1};
OS   Labilithrix luteola.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Sorangiineae; Labilitrichaceae; Labilithrix.
OX   NCBI_TaxID=1391654 {ECO:0000313|EMBL:AKU99279.1, ECO:0000313|Proteomes:UP000064967};
RN   [1] {ECO:0000313|EMBL:AKU99279.1, ECO:0000313|Proteomes:UP000064967}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27648 {ECO:0000313|EMBL:AKU99279.1,
RC   ECO:0000313|Proteomes:UP000064967};
RA   Babu N.S., Beckwith C.J., Beseler K.G., Brison A., Carone J.V.,
RA   Caskin T.P., Diamond M., Durham M.E., Foxe J.M., Go M.,
RA   Henderson B.A., Jones I.B., McGettigan J.A., Micheletti S.J.,
RA   Nasrallah M.E., Ortiz D., Piller C.R., Privatt S.R., Schneider S.L.,
RA   Sharp S., Smith T.C., Stanton J.D., Ullery H.E., Wilson R.J.,
RA   Serrano M.G., Buck G., Lee V., Wang Y., Carvalho R., Voegtly L.,
RA   Shi R., Duckworth R., Johnson A., Loviza R., Walstead R., Shah Z.,
RA   Kiflezghi M., Wade K., Ball S.L., Bradley K.W., Asai D.J.,
RA   Bowman C.A., Russell D.A., Pope W.H., Jacobs-Sera D., Hendrix R.W.,
RA   Hatfull G.F.;
RL   Submitted (AUG-2015) 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; CP012333; AKU99279.1; -; Genomic_DNA.
DR   EnsemblBacteria; AKU99279; AKU99279; AKJ09_05943.
DR   KEGG; llu:AKJ09_05943; -.
DR   PATRIC; fig|1391654.3.peg.6034; -.
DR   KO; K01580; -.
DR   Proteomes; UP000064967; 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:UP000064967};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000064967}.
FT   MOD_RES     274    274       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   464 AA;  52178 MW;  FDB355E53A4E5876 CRC64;
     MPLHARSEVS TNINDDVYAS TDLSVVMPKY KMAIYEHSAA HAYQVVHDEL MLDGNARMNL
     ATFCQTWSEP EVHKLMDECL DKNMIDKDEY PQTAELEARC VQMLADLWHA PEAADTMGCS
     TTGSSEAAML GGLALKWNWR KNRLAQKKSD AKPNLVCGPV QICWHKFARY FDVELRQIPL
     EPGQIGMTAK QIAQYCDENT IGVVPTLGVT FTLQYEPVEQ INRALDEIQK KTGLDIPIHV
     DAASGGFIAP FLHEDVKWDF QLPRVKSINA SGHKFGLTPL GCGWCVWREK SDLPEELIFN
     VDYLGGNMPT FALNFSRPGG QTAIQYYNFL RLGREGYRKI HQACAETAKF LAEEIRKIGA
     FDIVYDGIGG IPGVCWTLKK NGHPGNFTLY DIADRLRVRG WQVPAYPLPK NREDIIVQRV
     LIRHGVSRDL AKILVDDIKA SVGFFKGHPI TTPLNEKEGT SYHH
//
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