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Database: UniProt/TrEMBL
Entry: A0A126ZH58_9BURK
LinkDB: A0A126ZH58_9BURK
Original site: A0A126ZH58_9BURK 
ID   A0A126ZH58_9BURK        Unreviewed;       460 AA.
AC   A0A126ZH58;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   25-OCT-2017, entry version 13.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=AX767_20525 {ECO:0000313|EMBL:AMM26469.1};
OS   Variovorax sp. PAMC 28711.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=1795631 {ECO:0000313|EMBL:AMM26469.1, ECO:0000313|Proteomes:UP000070169};
RN   [1] {ECO:0000313|EMBL:AMM26469.1, ECO:0000313|Proteomes:UP000070169}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAMC 28711 {ECO:0000313|EMBL:AMM26469.1,
RC   ECO:0000313|Proteomes:UP000070169};
RA   Park H.;
RT   "Complete genome of Variovorax sp.";
RL   Submitted (FEB-2016) 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; CP014517; AMM26469.1; -; Genomic_DNA.
DR   RefSeq; WP_068633095.1; NZ_CP014517.1.
DR   EnsemblBacteria; AMM26469; AMM26469; AX767_20525.
DR   KEGG; vaa:AX767_20525; -.
DR   KO; K01580; -.
DR   Proteomes; UP000070169; 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:UP000070169};
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:UP000070169}.
FT   MOD_RES     274    274       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   460 AA;  51647 MW;  0E54ED2096550070 CRC64;
     MPIHHVDLDD QSSLRDIYAT KASQDSLPKY RLPQGRTEPR AAYALVRDEL LLDGNARQNL
     ATFCTTWIED EVKHLMADAI DKNMIDKDEY PQTAELESRC VHILADLWHA QQSRETVGCS
     TTGSSEAAML GGLAFKWKWR KRREAEGKDF SKPNIVTGPV QICWHKFARY FDVEIREVPL
     EGDALGLRPE DLRGHCDENT IGVVATLGVT FTGVYEPVEA LARELDAMQR DLGLDIPIHV
     DAASGGFIAP FIQRDLVWDF QIDRVRSINA SGHKYGLAPL GVGWVIWASK KDLAEELIFN
     VDYLGGNMPT FALNFSRPGG QIIAQYYNFL RLGWDGYTAV QQACSDTAQW LSAELAKLEP
     FEMVYDGHGG LPAVAYRLTD ADHGFTLYDL SERVRMRGWQ IASYPLPANR KDTVVQRILI
     RHGVSRDLAQ LLLDDIKRAL RDLTKNPVPN STAKPGFHHG
//
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