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Database: UniProt/TrEMBL
Entry: A0A0U3GE84_9GAMM
LinkDB: A0A0U3GE84_9GAMM
Original site: A0A0U3GE84_9GAMM 
ID   A0A0U3GE84_9GAMM        Unreviewed;       542 AA.
AC   A0A0U3GE84;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   07-JUN-2017, entry version 7.
DE   SubName: Full=Glutamate decarboxylase {ECO:0000313|EMBL:ALU43146.1};
GN   ORFNames=AT705_09445 {ECO:0000313|EMBL:ALU43146.1};
OS   Pseudoalteromonas rubra.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=43658 {ECO:0000313|EMBL:ALU43146.1, ECO:0000313|Proteomes:UP000069015};
RN   [1] {ECO:0000313|EMBL:ALU43146.1, ECO:0000313|Proteomes:UP000069015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCSIO 6842 {ECO:0000313|EMBL:ALU43146.1,
RC   ECO:0000313|Proteomes:UP000069015};
RA   Li B., Wang X.;
RT   "Complete genome sequence of Pseudoalteromonas rubra SCSIO 6842,
RT   harboring a conjugative plasmid.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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; CP013611; ALU43146.1; -; Genomic_DNA.
DR   RefSeq; WP_058796404.1; NZ_CP013611.1.
DR   EnsemblBacteria; ALU43146; ALU43146; AT705_09445.
DR   KEGG; prr:AT705_09445; -.
DR   KO; K01580; -.
DR   Proteomes; UP000069015; Chromosome 1.
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:UP000069015};
KW   Lyase {ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382}.
FT   MOD_RES     337    337       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   542 AA;  59902 MW;  92FAA7000E410239 CRC64;
     MGPKRCAVAS EESLMRIFTV PEAPSSTLSV IEQEISSNLA GFLNENIAAI EKPLHEIEKD
     FQSAMIPEEP MFVSDYAQDI MEQLVAHSVH TASPSFIGHM TSALPHFVLP LSKLMVGLNQ
     NLVKIETSKA FTPLERQVLG MMHHLAYGED DAFYEKWMHS AKTALGAFCS GGTIANISAL
     WIARNRLLGP DGDFKGLASE GIMAAMLHYG YKGLAVLVSE RGHYSLGKAA DVLGIGRSNF
     IAVKTDENNK VDVEAMRAKA QTLREQGIKV MAIVGVAGTT ETGNIDPLPE MAALAQDLGC
     HFHVDAAWGG ATLLSANYRH LLKGIELADS ITIDAHKQMY VPMGAGIVLF KDPTATDAIE
     HHAEYILRKG SKDLGSHTLE GSRPGMAMLV HACLRVIGRK GYEMLIDKGI EKAHYFAELI
     REEDDFELVS EPELCLLTYR YVPKQIRQAI EQADEQERID IYAALNRFTA SMQKRQRESG
     RSFVSRTRLT PSQYQYQPTV VFRVVLANPL TSKQMLKEIL AEQKGLAQSD PVFKKYLAKY
     MA
//
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