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Database: UniProt/TrEMBL
Entry: A0A0S2K4U2_9GAMM
LinkDB: A0A0S2K4U2_9GAMM
Original site: A0A0S2K4U2_9GAMM 
ID   A0A0S2K4U2_9GAMM        Unreviewed;       541 AA.
AC   A0A0S2K4U2;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   28-FEB-2018, entry version 9.
DE   SubName: Full=Glutamate decarboxylase {ECO:0000313|EMBL:ALO43329.1};
GN   ORFNames=PP2015_2844 {ECO:0000313|EMBL:ALO43329.1};
OS   Pseudoalteromonas phenolica.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=161398 {ECO:0000313|EMBL:ALO43329.1, ECO:0000313|Proteomes:UP000061457};
RN   [1] {ECO:0000313|EMBL:ALO43329.1, ECO:0000313|Proteomes:UP000061457}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 12086 {ECO:0000313|EMBL:ALO43329.1,
RC   ECO:0000313|Proteomes:UP000061457};
RA   Zhang Y., Guo Z.;
RL   Submitted (NOV-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; CP013187; ALO43329.1; -; Genomic_DNA.
DR   RefSeq; WP_058030994.1; NZ_CP013187.1.
DR   EnsemblBacteria; ALO43329; ALO43329; PP2015_2844.
DR   KEGG; pphe:PP2015_2844; -.
DR   PATRIC; fig|161398.10.peg.2903; -.
DR   KO; K01580; -.
DR   Proteomes; UP000061457; Chromosome I.
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   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.
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:UP000061457};
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:UP000061457}.
FT   MOD_RES     337    337       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   541 AA;  59588 MW;  54BC2B8271330820 CRC64;
     MGPKRCAVAS DETLMRIFTV PEAPDSTLSK IELEISNNLV GFLNENIAAI EKPLHEVEKD
     FQSAAIPEQP MFVSDYAQDI MEQLVAHSVH TASPSFIGHM TSALPHFVLP LSKLMVGLNQ
     NLVKIETSKA FTPLERQVLG MMHHLAYGAD ESFYGKWMHS AKTSLGAFCS GGTVANITAL
     WIARNRLLQP QGDFKGINSQ GLVAAMMHYG YKGLAVLVSE RGHYSLGKAA DVLGIGRDNF
     IAIKTSDDNK VDVQAMREKA LELEAQGIKV MALVGVAGTT ETGNIDPLSD MADLAQELNC
     HFHVDAAWGG ATLLSANARP LLAGIERADS ITIDAHKQMY VPMGAGMVLF KDPHATDAIE
     HHAEYILRKG SKDLGSHTLE GSRPGMAMLV HACLRVIGRQ GYEMLIDKGI AKAKYFAELI
     KQEEDFELVS EPELCLLTYR YVPKAIKQAI ANANEDEKID IYAALNRFTA SMQKRQREAG
     RSFVSRTRLT PVQYDNQPTV VFRVVLANPL TSEAMLKEIL DEQKQLAKTD PIFKKYLAKY
     I
//
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