(data stored in ACNUC10821 zone)

SWISSPROT: C8U1Q4_ECO10

ID   C8U1Q4_ECO10            Unreviewed;       713 AA.
AC   C8U1Q4;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   05-DEC-2018, entry version 45.
DE   SubName: Full=Lysine decarboxylase 2, constitutive {ECO:0000313|EMBL:BAI29062.1};
GN   Name=ldcC {ECO:0000313|EMBL:BAI29062.1};
GN   OrderedLocusNames=ECO103_0184 {ECO:0000313|EMBL:BAI29062.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29062.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29062.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
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DR   EMBL; AP010958; BAI29062.1; -; Genomic_DNA.
DR   RefSeq; WP_001020975.1; NC_013353.1.
DR   EnsemblBacteria; BAI29062; BAI29062; ECO103_0184.
DR   KEGG; eoh:ECO103_0184; -.
DR   HOGENOM; HOG000164394; -.
DR   KO; K01582; -.
DR   OMA; WSTLLTE; -.
DR   BioCyc; ECOL585395:ECO103_RS00940-MONOMER; -.
DR   Proteomes; UP000000959; 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; C8U1Q4.
DR   SWISS-2DPAGE; C8U1Q4.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
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;  80632 MW;  4482C6069744BBCE CRC64;
     MNIIAIMGPH GVFYKDEPIK ELESALVAQG FQIIWPQNSV DLLKFIEHNP RICGVIFDWD
     EYSLDLCSDI NQLNEYLPLY AFINTHSTMD VSVQDMRMAL WFFEYALGQA EDIAIRMRQY
     TDEYLDNITP PFTKALFTYV KERKYTFCTP GHMGGTAYQK SPVGCLFYDF FGGNTLKADV
     SISVTELGSL LDHTGPHLEA EEYIARTFGA EQSYIVTNGT STSNKIVGMY AAPSGSTLLI
     DRNCHKSLAH LLMMNDVVPV WLKPTRNALG ILGGIPRREF TRDSIEEKVA ATTQAQWPVH
     AVITNSTYDG LLYNTDWIKQ TLDVPSIHFD SAWVPYTHFH PIYQGKSGMS GERVAGKVIF
     ETQSTHKMLA ALSQASLIHI KGEYDEEAFN EAFMMHTTTS PSYPIVASVE TAAAMLRGNP
     GKRLINRSVE RALHFRKEVQ RLREESDGWF FDIWQPPQVD EAECWPVAPG EQWHGFNDAD
     ADHMFLDPVK VTILTPGMDE QGNMSEEGIP AALVAKFLDE RGIVVEKTGP YNLLFLFSIG
     IDKTKAMGLL RGLTEFKRSY DLNLRIKNML PDLYAEDPDF YRNMRIQDLA QGIHKLIRKH
     DLPGLMLRAF DTLPEMIMTP HQAWQRQIKG EVETIALEQL VGRVSANMIL PYPPGVPLLM
     PGEMLTKESR TVLDFLLMLC SVVQHYPGFE TDIHGAKQDE DGVYRVRVLK MAG
//

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