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Database: UniProt/TrEMBL
Entry: A0A0N9HZL8_9PSEU
LinkDB: A0A0N9HZL8_9PSEU
Original site: A0A0N9HZL8_9PSEU 
ID   A0A0N9HZL8_9PSEU        Unreviewed;       457 AA.
AC   A0A0N9HZL8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   25-OCT-2017, entry version 16.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=AOZ06_10750 {ECO:0000313|EMBL:ALG07339.1};
OS   Kibdelosporangium phytohabitans.
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Kibdelosporangium.
OX   NCBI_TaxID=860235 {ECO:0000313|EMBL:ALG07339.1, ECO:0000313|Proteomes:UP000063699};
RN   [1] {ECO:0000313|EMBL:ALG07339.1, ECO:0000313|Proteomes:UP000063699}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KLBMP1111 {ECO:0000313|EMBL:ALG07339.1,
RC   ECO:0000313|Proteomes:UP000063699};
RA   Qin S., Xing K.;
RT   "Genome sequencing of Kibdelosporangium phytohabitans.";
RL   Submitted (JUL-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:RU361171};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU361171}.
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DR   EMBL; CP012752; ALG07339.1; -; Genomic_DNA.
DR   RefSeq; WP_054289307.1; NZ_CP012752.1.
DR   EnsemblBacteria; ALG07339; ALG07339; AOZ06_10750.
DR   KEGG; kphy:AOZ06_10750; -.
DR   KO; K01580; -.
DR   Proteomes; UP000063699; 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:UP000063699};
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:UP000063699}.
FT   MOD_RES     273    273       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   457 AA;  49870 MW;  14AAC3C8AB432EAA CRC64;
     MALAHPSRGP EPGPSEVSVN PLYARVPTHI PKNELPAGGL DPDLAYQVVH DELMLDGNAR
     LNLATFVTTW MEPTAEKLMA ECFDKNMIDK DEYPRTAELE ARCVRMLAGL WHAPSVTDAP
     GCSTTGSSEA CMLAGLALKR RWRNRGGPGR PNIVMGVNVQ VCWEKFANYW DVDARLVPMD
     GDRFHLSAEE AVKLCDENTI GVVAVLGSTF DGSYEPVEEI CRALDEVQAG TGLDIPVHVD
     GASGAMIAPF CDPDLRWDFR LPRVASINTS GHKYGLVYPG VGWVVWRDTQ ALPEDLVFRV
     NYLGGTMPTF ALNFSRPGSQ VVTQYYNFLR LGFDGYRRVQ QACRDVATSL AARIAELGPL
     TLLTKGDELP VFAFTVAEGQ PFSVFNVSTA LRARGWQVPA YTFPANRTDL AALRIVVRNG
     FSPDLADALL ADLKQVLPAL ATLDHPKPGP SAFAHGT
//
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