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Database: UniProt/TrEMBL
Entry: W5WAX6_9PSEU
LinkDB: W5WAX6_9PSEU
Original site: W5WAX6_9PSEU 
ID   W5WAX6_9PSEU            Unreviewed;       467 AA.
AC   W5WAX6;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   25-OCT-2017, entry version 21.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=KALB_4720 {ECO:0000313|EMBL:AHH98082.1};
OS   Kutzneria albida DSM 43870.
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Kutzneria.
OX   NCBI_TaxID=1449976 {ECO:0000313|EMBL:AHH98082.1, ECO:0000313|Proteomes:UP000019225};
RN   [1] {ECO:0000313|EMBL:AHH98082.1, ECO:0000313|Proteomes:UP000019225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43870 {ECO:0000313|EMBL:AHH98082.1};
RX   PubMed=25301375; DOI=10.1186/1471-2164-15-885;
RA   Rebets Y., Tokovenko B., Lushchyk I., Ruckert C., Zaburannyi N.,
RA   Bechthold A., Kalinowski J., Luzhetskyy A.;
RT   "Complete genome sequence of producer of the glycopeptide antibiotic
RT   Aculeximycin Kutzneria albida DSM 43870T, a representative of minor
RT   genus of Pseudonocardiaceae.";
RL   BMC Genomics 15:885-885(2014).
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; CP007155; AHH98082.1; -; Genomic_DNA.
DR   RefSeq; WP_042220706.1; NZ_CP007155.1.
DR   EnsemblBacteria; AHH98082; AHH98082; KALB_4720.
DR   KEGG; kal:KALB_4720; -.
DR   PATRIC; fig|1449976.3.peg.4753; -.
DR   KO; K01580; -.
DR   Proteomes; UP000019225; 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:UP000019225};
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:UP000019225}.
FT   MOD_RES     278    278       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   467 AA;  51760 MW;  6D5D10B4D8DFB6FD CRC64;
     MPLSHPSQHS DSGRPELSIN PIFTREPLSV PRNRLPDAEL DPETAYQVVH DELMLDGNSR
     LNLATFVTTW MEPQAARLMA ECADKNMIDK DEYPRTAELE MRCVRMLAQL WHAPPAETAT
     GCSTTGSSEA CMLAGLALKR RWQHARRAQG KPTDRPNLVM GVNVQVCWDK FANYWDVEPR
     LVPMEGERFT LSAEEAVKLC DENTIGVVAI LGSTFDGSYE PVAEICAALD ELHERTGLDV
     PVHVDGASGA MVAPFCDPDL AWDFRLPRVA SINTSGHKYG LVYPGVGWVV WRDAEALPED
     LVFRVNYLGG DMPTFALNFS RPGAQVVAQY YNFLRLGFDG YRRVQQSCRE VATSLAARLA
     KLGAFRLITD GSQLPVVAFT LAEEVTGYSV FDVSAELRQH GWLVPAYTFP PDREDLSVLR
     LVVRNGFSHD LADLFLDDLE RVVGRLQQRS GPQRGPEAAG FAHGAGR
//
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