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Database: UniProt/TrEMBL
Entry: U4K3X4_9VIBR
LinkDB: U4K3X4_9VIBR
Original site: U4K3X4_9VIBR 
ID   U4K3X4_9VIBR            Unreviewed;       551 AA.
AC   U4K3X4;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   07-JUN-2017, entry version 21.
DE   SubName: Full=Putative decarboxylase {ECO:0000313|EMBL:CCO57261.1};
GN   ORFNames=VIBNI_A1113 {ECO:0000313|EMBL:CCO57261.1};
OS   Vibrio nigripulchritudo.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=28173 {ECO:0000313|EMBL:CCO57261.1, ECO:0000313|Proteomes:UP000016895};
RN   [1] {ECO:0000313|EMBL:CCO57261.1, ECO:0000313|Proteomes:UP000016895}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SnF1 {ECO:0000313|Proteomes:UP000016895};
RX   PubMed=23739050; DOI=10.1038/ismej.2013.90;
RA   Goudenege D., Labreuche Y., Krin E., Ansquer D., Mangenot S.,
RA   Calteau A., Medigue C., Mazel D., Polz M.F., Le Roux F.;
RT   "Comparative genomics of pathogenic lineages of Vibrio
RT   nigripulchritudo identifies virulence-associated traits.";
RL   ISME J. 7:1985-1996(2013).
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; FO203526; CCO57261.1; -; Genomic_DNA.
DR   RefSeq; WP_022550239.1; NC_022528.1.
DR   EnsemblBacteria; CCO57261; CCO57261; VIBNI_A1113.
DR   GeneID; 29463485; -.
DR   KEGG; vni:VIBNI_A1113; -.
DR   PATRIC; fig|1260221.3.peg.1075; -.
DR   KO; K01580; -.
DR   BioCyc; VNIG28173:G13HB-1071-MONOMER; -.
DR   Proteomes; UP000016895; 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:UP000016895};
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:UP000016895}.
FT   MOD_RES     338    338       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   551 AA;  61428 MW;  2E50F37018264D04 CRC64;
     MVSENKTADV SFESLLKIFT VPEAPDSTLG HIENKLSQNL NQFLREHIVA EEKPLADIEQ
     QFSNPYLPEQ PQFVSEHTQN LLDNLVSQSV HTSAPSFIGH MTSALPYFLM PLSKIMIALN
     QNLVKIETSK AFTPLERQVL GMLHGLIYHE KPEFYQQWMH SANHSLGAFC SGGTIANITA
     LWVARNNTLK ADGEFKGVEK EGLFKAMKHY GYEGLAILVS ERGHYSLKKA ADVLGLGQEC
     LVSVKTDSKN KLCPDDLEQK IALLKSQNIK PFAIVGVAGT TETGNIDPLE RIAVISQKHG
     CHFHVDAAWG GATLMSNNYR HLLKGIELAD SVTIDAHKQL YIPMGAGMVL FKDPSAMTAI
     EHHAQYILRK GSKDLGSHTL EGSRSGMAML VYSSMHIISR PGYELLIDQS IEKAKYFASL
     VSEQDDFELV TEPELCLLTY RYVPEVAKKA LVNANEDEKG ALHEALNNLT KQIQKKQRET
     GKTFVSRTRL NPVQWQHRNT IVFRVVLANP LTTHEILQSV LCEQREIAAG FPNLMTQVSE
     LSMEILNKKA S
//
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