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Database: UniProt/TrEMBL
Entry: A8FX14_SHESH
LinkDB: A8FX14_SHESH
Original site: A8FX14_SHESH 
ID   A8FX14_SHESH            Unreviewed;       550 AA.
AC   A8FX14;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 59.
DE   SubName: Full=Pyridoxal-dependent decarboxylase {ECO:0000313|EMBL:ABV37387.1};
GN   OrderedLocusNames=Ssed_2780 {ECO:0000313|EMBL:ABV37387.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV37387.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV37387.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV37387.1,
RC   ECO:0000313|Proteomes:UP000002015};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) 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; CP000821; ABV37387.1; -; Genomic_DNA.
DR   RefSeq; WP_012143117.1; NC_009831.1.
DR   ProteinModelPortal; A8FX14; -.
DR   STRING; 425104.Ssed_2780; -.
DR   EnsemblBacteria; ABV37387; ABV37387; Ssed_2780.
DR   KEGG; sse:Ssed_2780; -.
DR   eggNOG; ENOG4105DY8; Bacteria.
DR   eggNOG; COG0076; LUCA.
DR   HOGENOM; HOG000282553; -.
DR   KO; K01580; -.
DR   OMA; TVNPHKM; -.
DR   OrthoDB; POG091H05DC; -.
DR   BioCyc; SSED425104:GH7Q-2876-MONOMER; -.
DR   Proteomes; UP000002015; 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:UP000002015};
KW   Lyase {ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382}.
FT   MOD_RES     336    336       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   550 AA;  61233 MW;  4FD770E36B681AE3 CRC64;
     MTARQAKASE EALLRIFTIP EAPGSTLSVI EQNISQNLMG FLQESVVAVE KPLTEIERDF
     QEHQIPAAPK FVSDYADEMM KTLVAHSVHT SAPSFIGHMT SALPYFVLPL SKMMVGLNQN
     LVKIETSKAF TPLERQVLGM MHHLIYDENE TFYNSWMHSA NVSLGAFCSG GTVANITALW
     TARNQLLKAD GDFKGIAAQG LMKGLRHYGY NDLAILVSER GHYSLGKTAD LLGIGRENII
     QIPTSNDNRV DVDKMRVTAK ALERDNIKVM AIVGVAGTTE TGNIDPLDKL ATLAEELDCH
     FHVDAAWGGA SLLSKKYRHL LKGIERADSV TIDAHKQMYV PMGAGMVIFK DPTFANAIKH
     HAEYILRKGS KDLGSQTLEG SRPGMAMLVH ACLQIIGRDG YEILINNSLE KARYFAELIK
     TTDNFELVSE PELCLLTYRY VPESVQKAMQ QARTDGDIER LLQFNRLLDG LTKFVQKRQR
     EQGTSFVSRT RINPEHCHDI DVDLKSVVFR VVLANPLTTN EILQQVLVEQ TQIASTDKKF
     LPQLLELAAH
//
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