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Database: UniProt/TrEMBL
Entry: A0A1L7F865_9PSEU
LinkDB: A0A1L7F865_9PSEU
Original site: A0A1L7F865_9PSEU 
ID   A0A1L7F865_9PSEU        Unreviewed;       458 AA.
AC   A0A1L7F865;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   20-JUN-2018, entry version 11.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=UA75_14890 {ECO:0000313|EMBL:APU20988.1};
OS   Actinoalloteichus sp. GBA129-24.
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Actinoalloteichus.
OX   NCBI_TaxID=1612551 {ECO:0000313|EMBL:APU20988.1, ECO:0000313|Proteomes:UP000185506};
RN   [1] {ECO:0000313|EMBL:APU20988.1, ECO:0000313|Proteomes:UP000185506}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GBA129-24 {ECO:0000313|EMBL:APU20988.1,
RC   ECO:0000313|Proteomes:UP000185506};
RA   Ruckert C., Nouioui I., Willmese J., van Wezel G., Klenk H.-P.,
RA   Kalinowski J., Zotchev S.B.;
RT   "Complete genome sequence of Actinoalloteichus fjordicus DSM 46856
RT   (=GBA129-24).";
RL   Submitted (JUN-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; CP016077; APU20988.1; -; Genomic_DNA.
DR   RefSeq; WP_075740771.1; NZ_CP016077.1.
DR   KEGG; acti:UA75_14890; -.
DR   KO; K01580; -.
DR   Proteomes; UP000185506; 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   InterPro; IPR010107; Glutamate_decarboxylase.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
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:UP000185506};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU361171, ECO:0000313|EMBL:APU20988.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU361171};
KW   Reference proteome {ECO:0000313|Proteomes:UP000185506}.
FT   MOD_RES     274    274       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   458 AA;  50536 MW;  0FB49609FDDD2F6E CRC64;
     MVLHSGRRQG PTPQGAGNPF YGLADPAPGS EITLPHQRLG AGPVPPDAAL QLVRDELELD
     GSARLNLATF VTTWMEPQAR ELMNDCVAKN MIDKDEYPQT AELERRCVNI LADLWHAPEP
     ADVIGCSTTG SSEACMLAGM AFKRRWRGPG RPNLVMGANV QICWEKFCQY WEVEPRLVPM
     AGDRFHLSAD EAVARCDENT IGVVAILGST FDGSYEPVAE ITAALDGLQR RTGLDIPVHV
     DGASGAMIAP FLDPGLTWDF RLPRVASINT SGHKYGLVYP GVGWVLWRHR DRLPAELVFK
     VNYLGGEMPT FALNFSRPGA EVVAQYYTFA RLGREGFRAV QQAARDVATR LADQIAELGP
     FRLLTRGDEL PVFAFTTNER AAGFTVFDVS RRLRERGWQV PAYTFPADRE DLAVLRIVCR
     NGFTQDLGDL FVEELRRVLA DLDSSPGCGH ATETAFHH
//
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