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Database: UniProt/TrEMBL
Entry: Q74CG6_GEOSL
LinkDB: Q74CG6_GEOSL
Original site: Q74CG6_GEOSL 
ID   Q74CG6_GEOSL            Unreviewed;       552 AA.
AC   Q74CG6;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   07-JUN-2017, entry version 82.
DE   SubName: Full=Pyridoxal-5'-phosphate-dependent decarboxylase {ECO:0000313|EMBL:AAR35085.1};
GN   OrderedLocusNames=GSU1707 {ECO:0000313|EMBL:AAR35085.1};
OS   Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=243231 {ECO:0000313|EMBL:AAR35085.1, ECO:0000313|Proteomes:UP000000577};
RN   [1] {ECO:0000313|EMBL:AAR35085.1, ECO:0000313|Proteomes:UP000000577}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51573 / DSM 12127 / PCA
RC   {ECO:0000313|Proteomes:UP000000577};
RX   PubMed=14671304; DOI=10.1126/science.1088727;
RA   Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.,
RA   Heidelberg J.F., Wu D., Wu M., Ward N., Beanan M.J., Dodson R.J.,
RA   Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S.,
RA   Gwinn M., Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J.,
RA   Davidsen T.M., Zafar N., White O., Tran B., Romero C., Forberger H.A.,
RA   Weidman J., Khouri H., Feldblyum T.V., Utterback T.R., Van Aken S.E.,
RA   Lovley D.R., Fraser C.M.;
RT   "Genome of Geobacter sulfurreducens: metal reduction in subsurface
RT   environments.";
RL   Science 302:1967-1969(2003).
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; AE017180; AAR35085.1; -; Genomic_DNA.
DR   RefSeq; NP_952758.1; NC_002939.5.
DR   RefSeq; WP_010942351.1; NC_002939.5.
DR   ProteinModelPortal; Q74CG6; -.
DR   STRING; 243231.GSU1707; -.
DR   EnsemblBacteria; AAR35085; AAR35085; GSU1707.
DR   GeneID; 2685450; -.
DR   KEGG; gsu:GSU1707; -.
DR   PATRIC; fig|243231.5.peg.1752; -.
DR   eggNOG; ENOG4105DY8; Bacteria.
DR   eggNOG; COG0076; LUCA.
DR   HOGENOM; HOG000282553; -.
DR   InParanoid; Q74CG6; -.
DR   KO; K01580; -.
DR   OMA; TVNPHKM; -.
DR   OrthoDB; POG091H05DC; -.
DR   BioCyc; GSUL243231:GH27-1897-MONOMER; -.
DR   Proteomes; UP000000577; Chromosome.
DR   GO; GO:0016831; F:carboxy-lyase activity; ISS:TIGR.
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:UP000000577};
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:UP000000577}.
FT   MOD_RES     338    338       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   552 AA;  61160 MW;  BD22CB0295BE5A1C CRC64;
     MPKNRDAARA SLENLYRIFT VPEAPDSTLG AIDQAISGDV TGFLQTHIVA IERDLEDIEA
     NFSSFSIPEE PTYVSEYTEF VKENLVAHSV HTASPAFVGH MTSALPYFML PLARLMTALN
     QNVVKVETSK AFTPMERQVL AMLHHLVYRR DEDFYPSWIH NSRHALGAFC SGGTIANITA
     LWVARNRLFA PNGAFRGIAQ EGLARALKHR GADGIAVLVS ERGHYSLGKA TDLLGIGRDD
     LVKVKTDANN RIDLKALREE CRRFQDRNTL PLALVGIAGT TETGNVDPLE AMADLAQELG
     CHFHVDAAWG GPTLFSDRHR SLLKGIERAD SVTIDGHKQL YVPMGAGMVV FKDPTALSAI
     EHHANYILRH GSKDLGSHTL EGSRPGKAML VHAGFSIIGR KGYELLIDMG IERARTFADM
     IKQHPDFELI SEPELNILTY RYCPAAVQQT LHDVTDRERA DINALLDLVC QLLQKFQREA
     GKTFVSRTRL HVARHDRELT VLRVVLANPL TTDEILESVL AEQCELVQLP EIQAVLQQVE
     ELCTGLAKAA SW
//
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