GenomeNet

Database: UniProt/TrEMBL
Entry: A0A1D8BXF7_9PSEU
LinkDB: A0A1D8BXF7_9PSEU
Original site: A0A1D8BXF7_9PSEU 
ID   A0A1D8BXF7_9PSEU        Unreviewed;       459 AA.
AC   A0A1D8BXF7;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   25-OCT-2017, entry version 8.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=TL08_13370 {ECO:0000313|EMBL:AOS63488.1};
OS   Actinoalloteichus hymeniacidonis.
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Actinoalloteichus.
OX   NCBI_TaxID=340345 {ECO:0000313|EMBL:AOS63488.1, ECO:0000313|Proteomes:UP000095210};
RN   [1] {ECO:0000313|EMBL:AOS63488.1, ECO:0000313|Proteomes:UP000095210}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HPA177(T) (DSM 45092(T)) {ECO:0000313|Proteomes:UP000095210};
RA   Schaffert L., Albersmeier A., Winkler A., Kalinowski J., Zotchev S.,
RA   Ruckert C.;
RT   "Complete genome sequence of the type strain Actinoalloteichus
RT   hymeniacidonis DSM 45092.";
RL   Submitted (MAR-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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP014859; AOS63488.1; -; Genomic_DNA.
DR   RefSeq; WP_069849277.1; NZ_CP014859.1.
DR   EnsemblBacteria; AOS63488; AOS63488; TL08_13370.
DR   KEGG; ahm:TL08_13370; -.
DR   PATRIC; fig|340345.3.peg.2859; -.
DR   KO; K01580; -.
DR   Proteomes; UP000095210; 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:UP000095210};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU361171, ECO:0000313|EMBL:AOS63488.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU361171};
KW   Reference proteome {ECO:0000313|Proteomes:UP000095210}.
FT   MOD_RES     274    274       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   459 AA;  51203 MW;  9E0002DA7FEB5B97 CRC64;
     MPLHGGHRTG PERRGDSNPF YGVADPTAGA EMVLPQRALG RHPIPPDTAH RLVRDELRLD
     GSSRLNLATF VTTWMEDQAR ELMNECVDKN MIDKDEYPQT AELERRCVNI LADLWHAPNL
     DDVLGCSTTG SSEACMLAGM AFKRRWRGPG RPNLVMGANV QICWSKFCEY WEVEPRIVPM
     DGDRFHLDAA EAVARCDENT IGVVTILGST FDGSYDPVAQ IASALDDLQR RTGLDIPIHV
     DGASGAMIAP FLDPDLVWDF ALPRVASINT SGHKYGLVYP GVGWILWRHR ELLPSELVFA
     VDYLGGCMPT FALNFSRPGA EVVAQYYTFV RLGREGYRLV QQSARDVAVR LADHIGELGP
     FRLITRGEEL PVFAVAIAEG TDFTVFDVSK RLREHGWQVP AYTFPANRTD LSVLRVVCRN
     GFTHDLADLF VEDLKRVLTD LRQSPGVRAD PKHNTAFHH
//
DBGET integrated database retrieval system