(data stored in ACNUC7421 zone)

SWISSPROT: B7UJ87_ECO27

ID   B7UJ87_ECO27            Unreviewed;       713 AA.
AC   B7UJ87;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   05-DEC-2018, entry version 47.
DE   SubName: Full=Lysine decarboxylase 2, constitutive {ECO:0000313|EMBL:CAS07739.1};
GN   Name=ldcC {ECO:0000313|EMBL:CAS07739.1};
GN   OrderedLocusNames=E2348C_0191 {ECO:0000313|EMBL:CAS07739.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS07739.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS07739.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
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DR   EMBL; FM180568; CAS07739.1; -; Genomic_DNA.
DR   RefSeq; WP_001020955.1; NC_011601.1.
DR   EnsemblBacteria; CAS07739; CAS07739; E2348C_0191.
DR   KEGG; ecg:E2348C_0191; -.
DR   HOGENOM; HOG000164394; -.
DR   KO; K01582; -.
DR   OMA; WSTLLTE; -.
DR   BioCyc; ECOL574521:E2348C_RS00985-MONOMER; -.
DR   Proteomes; UP000008205; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR   CDD; cd00615; Orn_deC_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR005308; OKR_de-COase_N.
DR   InterPro; IPR011193; Orn/lys/arg_de-COase.
DR   InterPro; IPR000310; Orn/Lys/Arg_deCO2ase_major_dom.
DR   InterPro; IPR008286; Prn/Lys/Arg_de-COase_C.
DR   InterPro; IPR036633; Prn/Lys/Arg_de-COase_C_sf.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   Pfam; PF01276; OKR_DC_1; 1.
DR   Pfam; PF03711; OKR_DC_1_C; 1.
DR   Pfam; PF03709; OKR_DC_1_N; 1.
DR   PIRSF; PIRSF009393; Orn_decarb; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   SUPFAM; SSF55904; SSF55904; 1.
DR   PROSITE; PS00703; OKR_DC_1; 1.
PE   4: Predicted;
DR   PRODOM; B7UJ87.
DR   SWISS-2DPAGE; B7UJ87.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR009393-1}.
FT   DOMAIN      362    376       OKR_DC_1. {ECO:0000259|PROSITE:PS00703}.
FT   MOD_RES     367    367       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR009393-1}.
SQ   SEQUENCE   713 AA;  80437 MW;  59B6F65FBBCEF617 CRC64;
     MNIIAIMGPH GVFYKDEPIK ELESALVAQG FQIIWPQNSV DLLKFIEHNP RICGVIFDWD
     EYSLDLCSDI NQLNEYLPLY AFINTHSTMD VSVQDMRMAL WFFEYALGLA EDIAIRMRQY
     TNEYLDNITP PFTKALFTYV KERKYTFCTP GHMGGTAYQK SPVGCLFYDF FGGNTLKADV
     SISVTELGSL LDHTGPHLEA EEYIARTFGA EQSYIVTNGT STSNKIVGMY AAPSGSTLLI
     DRNCHKSLAH LLMMNDVVPV WLKPTRNALG ILGGIPRGEF TRDSIEEKVA ATTQAQWPVH
     AVITNSTYDG LLYNTDWIKQ TLDVPSIHFD SAWVPYTHFH PIYQGKSGMS GERVAGKVIF
     ETQSTHKMLA ALSQASLIHI KGEYDEEAFN EAFMMHTTTS PSYPIVASVE TAAAMLRGNP
     GKRLINRSVE RALHFRKEVQ RLREESDGWF FDIWQPPQVD EAECWPVAPG EQWHGFSDAD
     ANHMFLDPVK VTILTPGMDE QGNMSEEGIP AALVAKFLDE RGIVVEKTGP YNLLFLFSIG
     IDKTKAMGLL RGLTEFKRSY DLNLRIKNML PDLYAEDPDF YRNMRIQDLA QGIHKLIRKH
     DLSGLMLRAF DTLPEMIMTP HQAWQRQIKG EVETIALEQL VGRVSANMIL PYPPGVPLLM
     PGEMLTKESR TVLDFLLMLC SVGQHYPGFE TDIHGAKQDE DGVYRVRVLK MAG
//

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