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Database: UniProt/TrEMBL
Entry: E4PRK9_MARAH
LinkDB: E4PRK9_MARAH
Original site: E4PRK9_MARAH 
ID   E4PRK9_MARAH            Unreviewed;       558 AA.
AC   E4PRK9;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   22-NOV-2017, entry version 34.
DE   SubName: Full=Pyridoxal-dependent decarboxylase {ECO:0000313|EMBL:ADP99106.1};
GN   OrderedLocusNames=HP15_3342 {ECO:0000313|EMBL:ADP99106.1};
OS   Marinobacter adhaerens (strain HP15).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Marinobacter.
OX   NCBI_TaxID=225937 {ECO:0000313|EMBL:ADP99106.1, ECO:0000313|Proteomes:UP000007077};
RN   [1] {ECO:0000313|Proteomes:UP000007077}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HP15 {ECO:0000313|Proteomes:UP000007077};
RA   Gaerdes A.A.M., Kaeppel E., Shezad A., Seebah S., Teeling H.,
RA   Yarza P., Gloeckner F.O., Ullrich M.S.;
RT   "Complete genome sequence of Marinobacter adhaerens type strain
RT   (HP15).";
RL   Submitted (FEB-2010) 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; CP001978; ADP99106.1; -; Genomic_DNA.
DR   RefSeq; WP_014578527.1; NC_017506.1.
DR   STRING; 225937.HP15_3342; -.
DR   EnsemblBacteria; ADP99106; ADP99106; HP15_3342.
DR   GeneID; 34127973; -.
DR   KEGG; mad:HP15_3342; -.
DR   PATRIC; fig|225937.3.peg.3368; -.
DR   eggNOG; ENOG4105DY8; Bacteria.
DR   eggNOG; COG0076; LUCA.
DR   KO; K01580; -.
DR   OMA; TVNPHKM; -.
DR   OrthoDB; POG091H05DC; -.
DR   Proteomes; UP000007077; 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:UP000007077};
KW   Lyase {ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382}.
FT   MOD_RES     338    338       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   558 AA;  62358 MW;  D0B33DFA4D6A09F3 CRC64;
     MTGKKKSAQA SVEAMYRVFT VPEAPESTLS RIDQNISRNL AGFLQEHIVA VERDLSDVEK
     DFSDYSIPEK PVFVSEQAQF LLDKLVANSV HTASPAFIGH MTSALPYFML PLSKIMIALN
     QNLVKTETSK AFTPMERQVL GMIHRLVYQE DGAFYRKWMH DPRYALGAMC SGGTVANLTA
     LWVARNRAFP AEGSFRGLHQ EGLFRALKYY GYEGAAIVVS RRGHYSLRKA ADVLGLGRES
     LIPVDTDDEN RINTDALRDK CLELQRQKIK VMAICGVAGT TETGNVDPLD AMADIAREFG
     AHFHVDAAWG GPTLFSRTYK HLLRGIEKAD SVTFDAHKQL YVPMGVGLVV FRDPSLASAV
     EHHAQYIIRK GSRDLGSTTL EGSRPGMSML IHSGLKILAR EGYEILIDQG IDKAKTFAEM
     IEAEPDFELV TRPELNILTY RYCPENVQEA LACADPLQAE KLNTCLNRIT KFIQKTQRER
     GKAFVSRTRL EPARYYNFPC IVFRVVLANP LTTKEILADI LSEQRELSRD EGIEDEISIL
     HQMADAVLKQ AAPNARQA
//
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