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Database: UniProt/TrEMBL
Entry: Q39V49_GEOMG
LinkDB: Q39V49_GEOMG
Original site: Q39V49_GEOMG 
ID   Q39V49_GEOMG            Unreviewed;       550 AA.
AC   Q39V49;
DT   22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2005, sequence version 1.
DT   07-JUN-2017, entry version 75.
DE   SubName: Full=Pyridoxal-5'-phosphate-dependent decarboxylase {ECO:0000313|EMBL:ABB31875.1};
GN   OrderedLocusNames=Gmet_1644 {ECO:0000313|EMBL:ABB31875.1};
OS   Geobacter metallireducens (strain GS-15 / ATCC 53774 / DSM 7210).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=269799 {ECO:0000313|EMBL:ABB31875.1, ECO:0000313|Proteomes:UP000007073};
RN   [1] {ECO:0000313|EMBL:ABB31875.1, ECO:0000313|Proteomes:UP000007073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GS-15 / ATCC 53774 / DSM 7210
RC   {ECO:0000313|Proteomes:UP000007073};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Geobacter metallireducens GS-15.";
RL   Submitted (OCT-2005) 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; CP000148; ABB31875.1; -; Genomic_DNA.
DR   RefSeq; WP_004511420.1; NC_007517.1.
DR   STRING; 269799.Gmet_1644; -.
DR   DNASU; 3740413; -.
DR   EnsemblBacteria; ABB31875; ABB31875; Gmet_1644.
DR   KEGG; gme:Gmet_1644; -.
DR   eggNOG; ENOG4105DY8; Bacteria.
DR   eggNOG; COG0076; LUCA.
DR   HOGENOM; HOG000282553; -.
DR   KO; K01580; -.
DR   OMA; TVNPHKM; -.
DR   OrthoDB; POG091H05DC; -.
DR   BioCyc; GMET269799:GHNY-1690-MONOMER; -.
DR   Proteomes; UP000007073; 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:UP000007073};
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:UP000007073}.
FT   MOD_RES     338    338       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   550 AA;  60722 MW;  3A6F81B10475A03F CRC64;
     MPKNRDAARA SLENLYRIFT VPEAPDSTLG AIDQAIAGDV AGFLQTHIVA IERPLEEIEA
     DFSSFSIPEE PTYVSEYTEF VKENLVAHSV HTASPAFVGH MTSALPYFML PLARLMTALN
     QNVVKVETSK AFTPMERQVL AMLHHLVYGR NDDFYPQWIH NSQHALGAFC SGGTLANVTA
     LWVARNRLFA PDGEFRGIAQ EGLARALKHR GADGIAVLVS ERGHYSLGKA ADLLGIGRDD
     LIKIKTDANN RIDLKALREE CRRLQDRNTL PLALVGIAGT TETGNVDPLE AMADLAQELG
     CHFHVDAAWG GPTLFSDRHR HLLRGIERAD SVTIDGHKQL YVPMGAGMVV FKDPTALSAI
     EHHANYILRH GSKDLGSHTL EGSRPGKAML VHAGFSIIGR KGYELLIDMG IERARTFADM
     IQRHPDFELI SEPELNILTY RYCPPAIQQA LTDATAQQRA AINGLLDQVC QLLQKYQREA
     GKTFVSRTRL HVARHDMELT VLRVVLANPL TTDEILEAVL AEQCEIVRLP EIQALLRQAE
     ELCPGLAKAV
//
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