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Database: UniProt/TrEMBL
Entry: D4ZAE7_SHEVD
LinkDB: D4ZAE7_SHEVD
Original site: D4ZAE7_SHEVD 
ID   D4ZAE7_SHEVD            Unreviewed;       550 AA.
AC   D4ZAE7;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   07-JUN-2017, entry version 39.
DE   SubName: Full=Glutamate decarboxylase, putative {ECO:0000313|EMBL:BAJ02992.1};
GN   OrderedLocusNames=SVI_3021 {ECO:0000313|EMBL:BAJ02992.1};
OS   Shewanella violacea (strain JCM 10179 / CIP 106290 / LMG 19151 /
OS   DSS12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=637905 {ECO:0000313|EMBL:BAJ02992.1, ECO:0000313|Proteomes:UP000002350};
RN   [1] {ECO:0000313|Proteomes:UP000002350}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10179 / CIP 106290 / LMG 19151 / DSS12
RC   {ECO:0000313|Proteomes:UP000002350};
RX   PubMed=20458400; DOI=10.1039/c000396d;
RA   Aono E., Baba T., Ara T., Nishi T., Nakamichi T., Inamoto E.,
RA   Toyonaga H., Hasegawa M., Takai Y., Okumura Y., Baba M., Tomita M.,
RA   Kato C., Oshima T., Nakasone K., Mori H.;
RT   "Complete genome sequence and comparative analysis of Shewanella
RT   violacea, a psychrophilic and piezophilic bacterium from deep sea
RT   floor sediments.";
RL   Mol. Biosyst. 6:1216-1226(2010).
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; AP011177; BAJ02992.1; -; Genomic_DNA.
DR   STRING; 637905.SVI_3021; -.
DR   EnsemblBacteria; BAJ02992; BAJ02992; SVI_3021.
DR   KEGG; svo:SVI_3021; -.
DR   eggNOG; ENOG4105DY8; Bacteria.
DR   eggNOG; COG0076; LUCA.
DR   HOGENOM; HOG000282553; -.
DR   KO; K01580; -.
DR   OMA; TVNPHKM; -.
DR   OrthoDB; POG091H05DC; -.
DR   BioCyc; SVIO637905:GCRO-3126-MONOMER; -.
DR   Proteomes; UP000002350; Chromosome.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR022517; Asp_decarboxylase_pyridox.
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   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR03799; NOD_PanD_pyr; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000002350};
KW   Lyase {ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002350}.
FT   MOD_RES     338    338       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   550 AA;  61088 MW;  C0C217B220F60E5E CRC64;
     MSMTPRRATA SEEALLRIFT VPEAPDSTLS VIEKNISQNL MGFLQESVVA VEKPLSEIEL
     DFQQHQIPSA PQFVSDYADE MMKTLVAHSV HTSSPSFIGH MTSALPYFVL PLSKMMVGLN
     QNLVKIETSK AFTPLERQVL GMMHHLIYSE DDKFYKNWMH SANYSLGAFC SGGTIANITA
     LWTARNQLLK ADGDFKGVSA QGLMKGLRHY GYDDLAILVS ERGHYSLAKT ADLLGIGRDN
     IIQVPTSSDN KVDVDKMRAM AKQLDLDNIK VMAIVGVAGT TETGNIDPLD ELATLAVELN
     CHFHVDAAWG GASLLSNKYR HLLKGIERAD SVTIDAHKQM YVPMGAGMVI FKDPAFANAI
     KHHAEYILRK GSKDLGSQTL EGSRPGMAML VHACLQIIGR DGYEILINNS LEKARYFAEL
     IHGQDDFQLV SEPELCLLTY RYVPKSVQEA MQETRESGNT EKLIEFNSLL DGLTKFVQKR
     QREQGTSFVS RTRINPESRA SLNIQSVVFR VVLANPLTTR EILQQVLAEQ IEIAQQDNEF
     LPQLLALASN
//
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