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Database: UniProt/TrEMBL
Entry: W0E7B2_MARPU
LinkDB: W0E7B2_MARPU
Original site: W0E7B2_MARPU 
ID   W0E7B2_MARPU            Unreviewed;       462 AA.
AC   W0E7B2;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   05-JUL-2017, entry version 20.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=MARPU_15615 {ECO:0000313|EMBL:AHF05109.1};
OS   Marichromatium purpuratum 984.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Chromatiaceae; Marichromatium.
OX   NCBI_TaxID=765910 {ECO:0000313|EMBL:AHF05109.1, ECO:0000313|Proteomes:UP000005275};
RN   [1] {ECO:0000313|EMBL:AHF05109.1, ECO:0000313|Proteomes:UP000005275}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=984 {ECO:0000313|EMBL:AHF05109.1,
RC   ECO:0000313|Proteomes:UP000005275};
RG   DOE Joint Genome Institute;
RA   Bryant D.A., Huntemann M., Han J., Chen A., Kyrpides N.,
RA   Mavromatis K., Markowitz V., Palaniappan K., Ivanova N.,
RA   Schaumberg A., Pati A., Liolios K., Nordberg H.P., Cantor M.N.,
RA   Hua S.X., Woyke T.;
RL   Submitted (DEC-2013) 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; CP007031; AHF05109.1; -; Genomic_DNA.
DR   RefSeq; WP_005222898.1; NZ_CP007031.1.
DR   STRING; 765910.MarpuDRAFT_1360; -.
DR   EnsemblBacteria; AHF05109; AHF05109; MARPU_15615.
DR   KEGG; mpur:MARPU_15615; -.
DR   eggNOG; ENOG4105CVK; Bacteria.
DR   eggNOG; COG0076; LUCA.
DR   KO; K01580; -.
DR   Proteomes; UP000005275; 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:UP000005275};
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:UP000005275}.
FT   MOD_RES     277    277       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   462 AA;  51719 MW;  5930B91B99371F05 CRC64;
     MVTRKIESIS PEEQDALLAP AYARRRMLEG VPRYRLPEHE MAPETAHDLI HDELMLDGNA
     RLNLATFVTT WMEPQAERLM AEAFDKNLID KDEYPRTAEI EARCVNIVSD LFHAPEQGVG
     ASAIGSSEAV MLAGMALKWR WRARRRARGE DTHRPNLILG ANVQVVWEKF CRYWDVEPRY
     IPMEKGRYVI TPEEVIARTD AHTIGVVAIL GTTFTGEYEP IEAIHAALEA QNATTGWEIP
     MHVDAASGGF VAPFLDPELV WDFRLPLVKS INVSGHKYGL VYPGVGWVVW RSHEDLPEEL
     IFRVNYLGGD MPTFTLNFSR PGNQVVGQYY NFLRLGRAGY TQVMTALREV ATGLARGVAD
     LGPFELVSDA STIPVFAFKL RDEITDYSVF DISHKLRESG WQVPAYTMPE HAESVAVLRV
     VVREGFSADL AELLLADLAK AVAHFEGLRA HDPAPPTPSF AH
//
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