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Database: UniProt/TrEMBL
Entry: A0A1V0KSV7_9GAMM
LinkDB: A0A1V0KSV7_9GAMM
Original site: A0A1V0KSV7_9GAMM 
ID   A0A1V0KSV7_9GAMM        Unreviewed;       542 AA.
AC   A0A1V0KSV7;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-SEP-2017, entry version 4.
DE   SubName: Full=Glutamate decarboxylase {ECO:0000313|EMBL:ARD44836.1};
GN   ORFNames=A3Q33_11270 {ECO:0000313|EMBL:ARD44836.1};
OS   Colwellia sp. PAMC 21821.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=1816219 {ECO:0000313|EMBL:ARD44836.1, ECO:0000313|Proteomes:UP000192179};
RN   [1] {ECO:0000313|EMBL:ARD44836.1, ECO:0000313|Proteomes:UP000192179}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAMC 21821 {ECO:0000313|EMBL:ARD44836.1,
RC   ECO:0000313|Proteomes:UP000192179};
RA   Kim H.-W.;
RT   "Complete genome sequence of Colwellia sp. PAMC 21821.";
RL   Submitted (MAR-2016) 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; CP014943; ARD44836.1; -; Genomic_DNA.
DR   KEGG; colw:A3Q33_11270; -.
DR   KO; K01580; -.
DR   Proteomes; UP000192179; 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:UP000192179};
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:UP000192179}.
FT   MOD_RES     338    338       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   542 AA;  60212 MW;  DA96437A208264FE CRC64;
     MTVNKRTAKV SEESLHRIFT IPVAPNSTLG RIENEISQNL AGFLGAHIAA TEQALSEIEK
     DFADSQIPET PAFVSDHMHH LLDKLVSQSV HTSSPNFIGH MTSALPYFIL PLSKLMIGLN
     QNLVKIETSK AFTPMERQVL GMMHRLVYQD EEPFYQQWMH SANHSLGAFC SGGTVANLTA
     LWVARNNLLK PDGEFKGVAR EGLFKALKHY NYDGLAILVS ARGHYSLKKS ADVLGIGQDS
     VIAIPTDENN KIDCQLLEEK CQELARENIQ VLSIVGVAGT TETGNIDPLD KMADIAQRYN
     AHFHVDAAWG GATLLSNKYR PLLKGIELAD SVTIDAHKQM YVPMGAGLVV FKNPASVAAI
     EHHAEYILRK GSKDLGSHTL EGSRPGMAML VYAALHVISR PGYELLINSS IEKANYFAQL
     IEQHADFELV TKPELCLLTY RYNPSSVQKL LANASDVEQE NINVLLDKLT EFVQKRQREN
     GKSFVSRTRI EVKKYQGRKT LVFRVVLANP LTTQTILQDV LAEQTLLAQE SERFLPLLLS
     MT
//
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