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Database: UniProt/TrEMBL
Entry: A0A0H5NE61_NOCFR
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Original site: A0A0H5NE61_NOCFR 
ID   A0A0H5NE61_NOCFR        Unreviewed;       471 AA.
AC   A0A0H5NE61;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-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   Name=gadB {ECO:0000313|EMBL:CRY74150.1};
GN   ORFNames=ERS450000_00509 {ECO:0000313|EMBL:CRY74150.1};
OS   Nocardia farcinica.
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia.
OX   NCBI_TaxID=37329 {ECO:0000313|EMBL:CRY74150.1, ECO:0000313|Proteomes:UP000057820};
RN   [1] {ECO:0000313|EMBL:CRY74150.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NCTC11134 {ECO:0000313|EMBL:CRY74150.1};
RA   Informatics Pathogen;
RL   Submitted (MAR-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; LN868938; CRY74150.1; -; Genomic_DNA.
DR   RefSeq; WP_060590199.1; NZ_LN868938.1.
DR   EnsemblBacteria; CRY74150; CRY74150; ERS450000_00509.
DR   KEGG; nfr:ERS450000_00509; -.
DR   KO; K01580; -.
DR   Proteomes; UP000057820; Chromosome 1.
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:UP000057820};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU000382, ECO:0000313|EMBL:CRY74150.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382}.
FT   MOD_RES     278    278       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   471 AA;  51977 MW;  93057400765E6AB4 CRC64;
     MPLSHPSFPQ DPGPSEVAVN PVFTREPVSV PRDRLPAGEL DADIAYQVVH DELMLDGNAR
     LNLATFVTTW MEPSARVLMA ECFDKNMIDK DEYPRTADLE QRCVRMLADL WHAADPAHAT
     GCSTTGSSEA CMLAGLALKR RWQHRRRAAG LSTERPNLVM GANVQVCWEK FADYWDVEAR
     LVPMAGDRFH LTAEAALPHC DENTIGVVAV LGSTFDGSYE PVAEICAALD ELERQRGWDI
     PVHVDGASGA MVAPFCDPDL VWDFRLPRVA SVNTSGHKYG LVYPGVGWVV WRDAAALPED
     LIFRVNYLGG QMPTFALNFS RPGAQVVAQY YTFLRLGRSG YTRVQQYCRD VATRLADRIA
     ALGAFRLLTD GRQLPVFAFT LAEGETGYSV FDVSAALREQ GWLVPAYTFP ADREDLAVLR
     IVVRNGFSHD LADMLLDALA AVLPRLRAQD RPQHGPDTAT FAHGAQAPRG H
//
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