ID   B7MP46_ECO81            Unreviewed;       713 AA.
AC   B7MP46;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=Lysine decarboxylase 2, constitutive {ECO:0000313|EMBL:CAR06411.1};
DE            EC=4.1.1.18 {ECO:0000313|EMBL:CAR06411.1};
GN   Name=ldcC {ECO:0000313|EMBL:CAR06411.1};
GN   OrderedLocusNames=ECED1_0192 {ECO:0000313|EMBL:CAR06411.1};
OS   Escherichia coli O81 (strain ED1a).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585397 {ECO:0000313|EMBL:CAR06411.1, ECO:0000313|Proteomes:UP000000748};
RN   [1] {ECO:0000313|Proteomes:UP000000748}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ED1a {ECO:0000313|Proteomes:UP000000748};
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-I family.
CC       {ECO:0000256|ARBA:ARBA00010671}.
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DR   EMBL; CU928162; CAR06411.1; -; Genomic_DNA.
DR   RefSeq; WP_001020959.1; NC_011745.1.
DR   AlphaFoldDB; B7MP46; -.
DR   KEGG; ecq:ECED1_0192; -.
DR   HOGENOM; CLU_014292_3_0_6; -.
DR   Proteomes; UP000000748; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0008923; F:lysine decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   CDD; cd00615; Orn_deC_like; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.90.100.10; Orn/Lys/Arg decarboxylase, C-terminal domain; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR45229:SF3; BIODEGRADATIVE ARGININE DECARBOXYLASE; 1.
DR   PANTHER; PTHR45229; CONSTITUTIVE ORNITHINE DECARBOXYLASE; 1.
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; SSF55904; Ornithine decarboxylase C-terminal domain; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00703; OKR_DC_1; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:CAR06411.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR009393-1}.
FT   DOMAIN          362..376
FT                   /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT                   attachment site"
FT                   /evidence="ECO:0000259|PROSITE:PS00703"
FT   MOD_RES         367
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009393-1"
SQ   SEQUENCE   713 AA;  80403 MW;  2558CE3330E3D75F CRC64;
     MNIIAIMGPH GVFYKDEPIK ELESALVAQG FQIIWPQNSV DLLKFIEHNP RICGVIFDWD
     EYSLDLCSDI NQLNEYLPLY AFINTHSTMD VSVQDMRMAL WFFEYALGQA EDIAIRMRQC
     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
     DLPGLMLRAF DTLPEMIMTP HQAWQRQIKG EVETIALEQL VGRVSANMIL PYPPGVPLLM
     PGEMLTEESR TVLDFLLMLC SVGQHYPGFE TDIHGAKQDE DGVYRVRVLK MAG
//