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Database: UniProt/TrEMBL
Entry: F9ZR18_ACICS
LinkDB: F9ZR18_ACICS
Original site: F9ZR18_ACICS 
ID   F9ZR18_ACICS            Unreviewed;       458 AA.
AC   F9ZR18;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   25-OCT-2017, entry version 34.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   OrderedLocusNames=Atc_1674 {ECO:0000313|EMBL:AEK58322.1};
OS   Acidithiobacillus caldus (strain SM-1).
OC   Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales;
OC   Acidithiobacillaceae; Acidithiobacillus.
OX   NCBI_TaxID=990288 {ECO:0000313|EMBL:AEK58322.1, ECO:0000313|Proteomes:UP000006135};
RN   [1] {ECO:0000313|EMBL:AEK58322.1, ECO:0000313|Proteomes:UP000006135}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM-1 {ECO:0000313|EMBL:AEK58322.1,
RC   ECO:0000313|Proteomes:UP000006135};
RX   PubMed=21703548; DOI=10.1016/j.jgg.2011.04.006;
RA   You X.Y., Guo X., Zheng H.J., Zhang M.J., Liu L.J., Zhu Y.Q., Zhu B.,
RA   Wang S.Y., Zhao G.P., Poetsch A., Jiang C.Y., Liu S.J.;
RT   "Unraveling the Acidithiobacillus caldus complete genome and its
RT   central metabolisms for carbon assimilation.";
RL   J. Genet. Genomics 38:243-252(2011).
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; CP002573; AEK58322.1; -; Genomic_DNA.
DR   RefSeq; WP_004872263.1; NC_015850.1.
DR   ProteinModelPortal; F9ZR18; -.
DR   EnsemblBacteria; AEK58322; AEK58322; Atc_1674.
DR   KEGG; acu:Atc_1674; -.
DR   KO; K01580; -.
DR   OMA; RPNLVMG; -.
DR   OrthoDB; POG091H06F5; -.
DR   Proteomes; UP000006135; 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:UP000006135};
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:UP000006135}.
FT   MOD_RES     273    273       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   458 AA;  51770 MW;  D4B2B2FBBEA0A4D0 CRC64;
     MVKSWQEEDG VLQPAFASRS MDCSVPKYRL PDKEMDARTA YQLIHDELML DGNARLNLAT
     FVTTWMEPEA ERLMAETFDK NMIDKDEYPQ TAEIESRCVN MLARLFHAPQ QGKAVGVSAI
     GSSEAVMLAG MALKWRWRQE REKAGQSAQR PNLVLGRNVQ VVWEKFCRYW EVEPRYLPMK
     EGRYTLSPEA VVAAVDAHTI GVVAVLGTTF TGEYDPVAAI HEALVPLTEK LGRPVPIHVD
     AASGGFVAPF LQPDLAWDFR LPQVVSINCS GHKYGLVYPG VGWALWRDRD FLPDELIFHV
     NYLGGDMPTF TLNFSRPGNQ IVGQYYNFLR LGREGYTRIL KNLQDTALWL AKALEGMGIF
     QVIGGGDTIP VIALRLRQDV RHYDVFAISD ALRRRGWQVP AYTLPADCED IAILRLVIRE
     GFSRDLAELL LKDFKEAVHE LDHGNAHARV HKPVFHHN
//
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