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Database: UniProt/TrEMBL
Entry: A0A0S2KBH9_9GAMM
LinkDB: A0A0S2KBH9_9GAMM
Original site: A0A0S2KBH9_9GAMM 
ID   A0A0S2KBH9_9GAMM        Unreviewed;       547 AA.
AC   A0A0S2KBH9;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   07-JUN-2017, entry version 9.
DE   SubName: Full=Glutamate decarboxylase {ECO:0000313|EMBL:ALO45691.1};
GN   ORFNames=PS2015_1026 {ECO:0000313|EMBL:ALO45691.1};
OS   Pseudohongiella spirulinae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudohongiella.
OX   NCBI_TaxID=1249552 {ECO:0000313|EMBL:ALO45691.1, ECO:0000313|Proteomes:UP000065641};
RN   [1] {ECO:0000313|EMBL:ALO45691.1, ECO:0000313|Proteomes:UP000065641}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 32221 {ECO:0000313|EMBL:ALO45691.1,
RC   ECO:0000313|Proteomes:UP000065641};
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; CP013189; ALO45691.1; -; Genomic_DNA.
DR   RefSeq; WP_058021209.1; NZ_CP013189.1.
DR   EnsemblBacteria; ALO45691; ALO45691; PS2015_1026.
DR   KEGG; pspi:PS2015_1026; -.
DR   PATRIC; fig|1249552.3.peg.1032; -.
DR   KO; K01580; -.
DR   Proteomes; UP000065641; 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:UP000065641};
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:UP000065641}.
FT   MOD_RES     338    338       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   547 AA;  60170 MW;  FC2FC933EDC745F4 CRC64;
     MSESKKLASA SLESLYRIFT VPEAPDSTLG RIDQSISQNL AGFLQEHIVA SERDLSDIEK
     DFADPQIPEQ PTFVSDQIQF VLDKLVAQSV HISAPSFVGH MASALPYFML PLSRIMMALN
     QNLVKVETSK AFTPMERQVV GMIHHLVYGR DKDFYTQWMH DRAHALGSFC SGGTIANLTA
     LWAARNNVLA PTEGFAGLGQ EGLVAGMQHY GYKGLAILVS ERGHYSLGKA ADILGIGRRS
     LIAIETDANN KIRTDLLAKK CDELAAANIK VMAIVGIAGA SETGSIDPLD QMADIAQERG
     IHFHVDSAWG GPTLFSNTYR PLLKGIERAD SVTLDAHKQL YVPMGAGICV FKEPSTLSSV
     EHHAEYIIRK GSKDLGSHTV EGSRPGMAIL VHSGLHIIGR QGYELLIDQG ISRARHFADM
     IRADKDFELI SEPELNILTY RYVPQDIQTA LESAPASLRT EVNEQLNLVT KRIQKTQRGL
     GRSFVSRTRL NPHHHNRNAV IVFRAVLANP LTTNQILQDM LAEQKEIAAT PPIQALLKQV
     RNLFCGC
//
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