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Database: UniProt/TrEMBL
Entry: B8J1X0_DESDA
LinkDB: B8J1X0_DESDA
Original site: B8J1X0_DESDA 
ID   B8J1X0_DESDA            Unreviewed;       468 AA.
AC   B8J1X0;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   25-OCT-2017, entry version 49.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   OrderedLocusNames=Ddes_0045 {ECO:0000313|EMBL:ACL47965.1};
OS   Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=525146 {ECO:0000313|EMBL:ACL47965.1, ECO:0000313|Proteomes:UP000002598};
RN   [1] {ECO:0000313|EMBL:ACL47965.1, ECO:0000313|Proteomes:UP000002598}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27774 / DSM 6949 {ECO:0000313|Proteomes:UP000002598};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Lu M., Kiss H., Meineke L.,
RA   Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Ovchinnikova G., Hazen T.C.;
RT   "Complete sequence of Desulfovibrio desulfuricans subsp. desulfuricans
RT   str. ATCC 27774.";
RL   Submitted (JAN-2009) 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; CP001358; ACL47965.1; -; Genomic_DNA.
DR   RefSeq; WP_012623697.1; NC_011883.1.
DR   STRING; 525146.Ddes_0045; -.
DR   EnsemblBacteria; ACL47965; ACL47965; Ddes_0045.
DR   KEGG; dds:Ddes_0045; -.
DR   eggNOG; ENOG4105CVK; Bacteria.
DR   eggNOG; COG0076; LUCA.
DR   HOGENOM; HOG000070228; -.
DR   KO; K01580; -.
DR   OMA; RPNLVMG; -.
DR   OrthoDB; POG091H06F5; -.
DR   BioCyc; DDES525146:GIWF-45-MONOMER; -.
DR   Proteomes; UP000002598; 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:UP000002598};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU361171, ECO:0000313|EMBL:ACL47965.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU361171};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002598}.
FT   MOD_RES     272    272       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   468 AA;  52796 MW;  4E505D0BF8A593B1 CRC64;
     MTAKNTLRNT VLDDTYAASD MANAMPRHEM PQQESRPRDV YQAIHDELML DGNSRQNLAT
     FCQTWVDPEI NQIMAECVDK NMIDKDEYPQ TAETETRCVH MLADLWHSPD PKGTLGCSTT
     GSSEAAMLGG LAMKRRWVNM RKAAGKPYDK PNMVCGPVQV CWEKFARYWD VELREIPMEK
     DRLIMTAEEV IKRCDENTIG VVPTLGVTFT GQYEPVEEVS KALDKLQKDK GWDIPIHVDG
     ASGGFLAPFI EPDLLWDFRL PRVKSINSSG HKFGLAPLGV GWVVWREKSD LPEDLIFNVN
     YLGGNMPTFA LNFSRPGGQI IAQYYNFLRL GREGYRRIHQ NCYDTARFLG DEIAKLGPFE
     VLYNGRGGIP ALCWTFKANA KTSYSLYDLS DRLRSRGWQV PAYSMPAHRE DLVVMRVLVR
     HGFSRDLGSL LVDDLKRAMA HFDAHPVSKP LSETEAGSNS HAGRAAKK
//
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