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Database: UniProt/TrEMBL
Entry: B9M3A1_GEODF
LinkDB: B9M3A1_GEODF
Original site: B9M3A1_GEODF 
ID   B9M3A1_GEODF            Unreviewed;       556 AA.
AC   B9M3A1;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   07-JUN-2017, entry version 52.
DE   SubName: Full=Pyridoxal-5'-phosphate-dependent decarboxylase {ECO:0000313|EMBL:ACM19511.1};
GN   OrderedLocusNames=Geob_1151 {ECO:0000313|EMBL:ACM19511.1};
OS   Geobacter daltonii (strain DSM 22248 / JCM 15807 / FRC-32).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=316067 {ECO:0000313|EMBL:ACM19511.1, ECO:0000313|Proteomes:UP000007721};
RN   [1] {ECO:0000313|EMBL:ACM19511.1, ECO:0000313|Proteomes:UP000007721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22248 / JCM 15807 / FRC-32
RC   {ECO:0000313|Proteomes:UP000007721};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Kostka J., Richardson P.;
RT   "Complete sequence of Geobacter sp. FRC-32.";
RL   Submitted (JAN-2009) 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; CP001390; ACM19511.1; -; Genomic_DNA.
DR   RefSeq; WP_012646240.1; NC_011979.1.
DR   ProteinModelPortal; B9M3A1; -.
DR   STRING; 316067.Geob_1151; -.
DR   EnsemblBacteria; ACM19511; ACM19511; Geob_1151.
DR   KEGG; geo:Geob_1151; -.
DR   eggNOG; ENOG4105DY8; Bacteria.
DR   eggNOG; COG0076; LUCA.
DR   HOGENOM; HOG000282553; -.
DR   KO; K01580; -.
DR   OMA; TVNPHKM; -.
DR   OrthoDB; POG091H05DC; -.
DR   BioCyc; GDAL316067:G12WX-1144-MONOMER; -.
DR   Proteomes; UP000007721; 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:UP000007721};
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:UP000007721}.
FT   MOD_RES     338    338       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   556 AA;  60908 MW;  0238BBFE25959B0D CRC64;
     MLKNREAARA NLENLYRIFT VPEAPDSTLG AIDQAIAADV TGFLQTHIVA IERDLEAIEA
     DFASAIIPEE PTYVSEYTEF VKENLVAQSV HTAAPGFVGH MTSAIPYFML PLARLMTALN
     QNLVKVETSK AFTPMERQVL AMLHHLVYRR DADFYPAWIH NSQHALGAFC SGGTIANVTA
     LWVARNRLFA PSADFGGLAQ EGLGRALQHR GAEGIAVLVS ERGHYSFGKA ADLLGLGRDN
     LIKVQTDAHN RVDLKLLREE VRRLQDRNIL PLALVGIAGT TETGNVDPLE ALADLAGELG
     CHFHVDAAWG GPTLFSDRFR SLLSGIERAD SVTIDAHKQL YVPMGAGMVV FKDPTALSAI
     EHHANYILRH GSKDLGSHTL EGSRPGMAML VHAGLSIIGR KGYELLMDMG IERARTFAAM
     IRQYPDFELT SEPELNILTY RYCPLNVQKA LAAAPAEQRA GINALLDQVC QLLQKHQREA
     GKTFVSRTRL RVARHDEELT VLRVVLANPL TTDEILAAVL AEQCEIVQQP EIQGLLQQVE
     EICTGLTAKA ADQSPN
//
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