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Database: UniProt/TrEMBL
Entry: A0A075V5W6_9PSEU
LinkDB: A0A075V5W6_9PSEU
Original site: A0A075V5W6_9PSEU 
ID   A0A075V5W6_9PSEU        Unreviewed;       457 AA.
AC   A0A075V5W6;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   25-OCT-2017, entry version 18.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=AJAP_39845 {ECO:0000313|EMBL:AIG80748.1};
OS   Amycolatopsis japonica.
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Amycolatopsis.
OX   NCBI_TaxID=208439 {ECO:0000313|EMBL:AIG80748.1, ECO:0000313|Proteomes:UP000028492};
RN   [1] {ECO:0000313|EMBL:AIG80748.1, ECO:0000313|Proteomes:UP000028492}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MG417-CF17 (DSM 44213) {ECO:0000313|Proteomes:UP000028492};
RX   PubMed=25193710;
RA   Stegmann E., Albersmeier A., Spohn M., Gert H., Weber T.,
RA   Wohlleben W., Kalinowski J., Ruckert C.;
RT   "Complete genome sequence of the actinobacterium Amycolatopsis
RT   japonica MG417-CF17(T) (=DSM 44213T) producing (S,S)-N,N'-
RT   ethylenediaminedisuccinic acid.";
RL   J. Biotechnol. 0:0-0(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; CP008953; AIG80748.1; -; Genomic_DNA.
DR   RefSeq; WP_038521098.1; NZ_CP008953.1.
DR   EnsemblBacteria; AIG80748; AIG80748; AJAP_39845.
DR   GeneID; 29584988; -.
DR   KEGG; aja:AJAP_39845; -.
DR   KO; K01580; -.
DR   Proteomes; UP000028492; 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:UP000028492};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU361171, ECO:0000313|EMBL:AIG80748.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU361171}.
FT   MOD_RES     277    277       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   457 AA;  50764 MW;  A1DEB677E12A0997 CRC64;
     MVLHKGTASD PDRKTGANPL YAGAYPALAA NIRLPHDSLA EDPLPPDTAL QLVRDELMLD
     GNARLNLATF VTTWMEPQAR ELMAECVDKN MIDKDEYPQT AELERRCVNI LADLWHAPDP
     TAIMGCSTTG SSEACMLAGM ALKRRWSKLG RTGKPNLVMG ANVQVCWEKF CEYWEVEPRL
     VPMDGDRFHL TADEAIARCD ENTIGVVAIL GSTFDGSYEP VAEIAAALDG LAERSGWDIP
     VHVDGASGAM IAPFLDPELS WDFRLPRVAS INTSGHKYGL VYPGVGWVLW RDKDALPEEL
     VFNVNYLGGD MPTFALNFSR PGAEVAAQYY TFVRLGREGF RAVQQASRDV ATQLADGIAE
     LGPFRLLTRG DQLPVFAFTT KPDVEGFDVF DVSRRLRERG WLVPAYTFPE NRTDLAVLRI
     VVRNGFTHDL AELLLADLRR LLPELDHGPR RRTAFHH
//
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