ID   LDCI_SALTI              Reviewed;         714 AA.
AC   P0A1Z1; Q60002;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Inducible lysine decarboxylase;
DE            Short=LDC;
DE            EC=4.1.1.18;
GN   Name=cadA; Synonyms=ldcI; OrderedLocusNames=STY2806, t0297;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA   Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT   CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-lysine = cadaverine + CO2; Xref=Rhea:RHEA:22352,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:32551,
CC         ChEBI:CHEBI:58384; EC=4.1.1.18;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homodecamer. Interacts with RavA. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-I family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL513382; CAD02762.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO68022.1; -; Genomic_DNA.
DR   RefSeq; NP_457089.1; NC_003198.1.
DR   RefSeq; WP_001100652.1; NZ_WSUR01000007.1.
DR   AlphaFoldDB; P0A1Z1; -.
DR   SMR; P0A1Z1; -.
DR   STRING; 220341.16503772; -.
DR   EnsemblBacteria; AAO68022; AAO68022; t0297.
DR   KEGG; stt:t0297; -.
DR   KEGG; sty:STY2806; -.
DR   PATRIC; fig|220341.7.peg.2853; -.
DR   eggNOG; COG1982; Bacteria.
DR   HOGENOM; CLU_014292_3_0_6; -.
DR   OMA; NCHKSVF; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008923; F:lysine decarboxylase activity; IEA:UniProtKB-EC.
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; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
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   3: Inferred from homology;
KW   Cytoplasm; Decarboxylase; Lyase; Pyridoxal phosphate.
FT   CHAIN           1..714
FT                   /note="Inducible lysine decarboxylase"
FT                   /id="PRO_0000201140"
FT   MOD_RES         367
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   714 AA;  81235 MW;  01825527DE3EDDFC CRC64;
     MNVIAIMNHM GVYFKEEPIR ELHRALEGLN FRIVYPNDRE DLLKLIENNS RLCGVIFDWD
     KYNLELCEEI SKLNEYMPLY AFANSYSTLD VSLNDLRMQV RFFEYALGAA ADIAAKIRQN
     TDEYIDNILP PLTKALFKYV REGKYTFCTP GHMGGTAFQK SPVGSIFYDF FGPNTMKSDI
     SISVSELGSL LDHSGPHKEA EEYIARVFNA ERSYMVTNGT STANKIVGMY SAPAGSTVLI
     DRNCHKSLTH LMMMSDITPI YFRPTRNAYG ILGGIPQSEF QHATIAKRVK ETPNATWPVH
     AVITNSTYDG LLYNTDYIKK TLDVKSIHFD SAWVPYTNFS PIYQGKCGMS GDRVEGKIIY
     ETQSTHKLLA AFSQASMIHV KGDINEETFN EAYMMHTTTS PHYGIVASTE TAAAMMKGNA
     GKRLINGSIE RAIKFRKEIK RLKSESDGWF FDVWQPEHID GAECWPLRSD SAWHGFKNID
     NEHMYLDPIK VTILTPGMKK DGTMDEFGIP ASLVAKYLDE RGIIVEKTGP YNLLFLFSIG
     IDKTKALSLL RALTEFKRAF DLNLRVKNIL PALYREAPEF YENMRIQELA QNIHKLVEHH
     NLPDLMYRAF EVLPKMVMTP YTAFQKELHG ETEEVYLEEM VGRVNANMIL PYPPGVPLVM
     PGEMITEESR PVLEFLQMLC EIGAHYPGFE TDIHGAYRQA DGRYTVKVLK ENTK