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Database: UniProt/TrEMBL
Entry: A0A0F7FVD4_9ACTN
LinkDB: A0A0F7FVD4_9ACTN
Original site: A0A0F7FVD4_9ACTN 
ID   A0A0F7FVD4_9ACTN        Unreviewed;       454 AA.
AC   A0A0F7FVD4;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   25-OCT-2017, entry version 15.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=SXIM_28140 {ECO:0000313|EMBL:AKG44198.1};
OS   Streptomyces xiamenensis.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=408015 {ECO:0000313|EMBL:AKG44198.1, ECO:0000313|Proteomes:UP000034034};
RN   [1] {ECO:0000313|EMBL:AKG44198.1, ECO:0000313|Proteomes:UP000034034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCCC 1A01550 {ECO:0000313|Proteomes:UP000034034};
RA   Xu J.;
RT   "Complete genome sequence of a mangrove-derived Streptomyces
RT   xiamenensis.";
RL   Submitted (FEB-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; CP009922; AKG44198.1; -; Genomic_DNA.
DR   EnsemblBacteria; AKG44198; AKG44198; SXIM_28140.
DR   KEGG; sxi:SXIM_28140; -.
DR   PATRIC; fig|408015.6.peg.2851; -.
DR   KO; K01580; -.
DR   Proteomes; UP000034034; 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:UP000034034};
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:UP000034034}.
FT   MOD_RES     269    269       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   454 AA;  49826 MW;  E3221C9ADA1CEB68 CRC64;
     MTQERTDQAD DLYALPGSGR ALPRYTLPEG PMPAREAYQL IRDELALDGN SRQNLATFCT
     TWSEPEIRAL MTETLDKNMV DKDEYPQTAE LESRCVHILA ALWHAPHGEA AVGCSTTGSS
     EAAMLGGLAL HRRWRARREA AGLPADRPNL VCGPVQVCWE KFARYFDIEL RQMPLLPGRT
     TADPAQLARY CDERTIGVVA TLGVTFTGAY EPVEDIAAAL DALAARTGVD IPIHVDAASG
     GFVAPFLQPG LKWDFRVPRV KSVNCSGHKF GLAPLGVGWV VWRDAAELPA ELVFHVDYLG
     GDMPTFALNF SRPGGEIVAQ YYNLLRLGRA GYQAVQRACA DTAVALADSL AALGPFRVLH
     DGRAGLPVVC WTLAPDHSTW TLYDLAERLR LRGWQVPTYP LPADRQETVV QRVVVRHGVS
     RDLVQLLLED MRGALAELGR HPAATAEQRP AFHH
//
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