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Database: UniProt/TrEMBL
Entry: M1PNC0_DESSD
LinkDB: M1PNC0_DESSD
Original site: M1PNC0_DESSD 
ID   M1PNC0_DESSD            Unreviewed;       465 AA.
AC   M1PNC0;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   05-JUL-2017, entry version 28.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   OrderedLocusNames=UWK_01365 {ECO:0000313|EMBL:AGF77926.1};
OS   Desulfocapsa sulfexigens (strain DSM 10523 / SB164P1).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC   Desulfobulbaceae; Desulfocapsa.
OX   NCBI_TaxID=1167006 {ECO:0000313|EMBL:AGF77926.1, ECO:0000313|Proteomes:UP000011721};
RN   [1] {ECO:0000313|Proteomes:UP000011721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10523 / SB164P1 {ECO:0000313|Proteomes:UP000011721};
RX   DOI=10.4056/sigs.3777412;
RA   Finster K.W., Kjeldsen K.U., Kube M., Reinhardt R., Mussmann M.,
RA   Amann R., Schreiber L.;
RT   "Complete genome sequence of Desulfocapsa sulfexigens, a marine
RT   deltaproteobacterium specialized in disproportionating inorganic
RT   sulfur compounds.";
RL   Stand. Genomic Sci. 8:0-0(2013).
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:RU000382};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU000382}.
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DR   EMBL; CP003985; AGF77926.1; -; Genomic_DNA.
DR   RefSeq; WP_015403617.1; NC_020304.1.
DR   EnsemblBacteria; AGF77926; AGF77926; UWK_01365.
DR   KEGG; dsf:UWK_01365; -.
DR   PATRIC; fig|1167006.5.peg.1505; -.
DR   KO; K01580; -.
DR   OMA; FTTSVYG; -.
DR   OrthoDB; POG091H06F5; -.
DR   BioCyc; DSUL1167006:G135B-1353-MONOMER; -.
DR   Proteomes; UP000011721; 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:UP000011721};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU000382, ECO:0000313|EMBL:AGF77926.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011721}.
FT   MOD_RES     277    277       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   465 AA;  52824 MW;  DBB3DCBC99AC9E4D CRC64;
     MFVKKSQKEL EDHANIQPTY GSRTMREEIP KYELPDEGMP PTAAYNIIHD ELALDGNSRL
     NLATFVTTWM EPEARQLMTE TFDKNMIDKD EYPQTAEIEL RCVNILSRLW SSPEGEEAVG
     CSTIGSSEAA MLAGMALKRK WKHRMQAAGK PTDKPNFIMG RNVQVCWEKF CNYWEVEPRF
     VMAEGNSFNL RPEDAIELCD ENTIGVLAIM GSTFDGSYEP VAELNAALDA FYEKSGLDIP
     IHVDAASGGF VAPFLQPELM WDFRVPRVKS INVSGHKYGL VYPGVGWAIW RDKKELPEEL
     IFHCDYLGGD LPNFALNFSR PGNQVIAQYY NFLRLGLDGY TAIQETCREI ALFLSSNIAK
     IGPFELISKG DTIPVFAWKL KDHFADTANF SLFDLAERLR YNGWLVPAYR MPENRKDLIV
     QRIVVKEGFS RDMAGALLAD IQKHVQWFAD HPGFNRTMEG KQFSH
//
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