LDCI_SALTY
ID LDCI_SALTY Reviewed; 714 AA.
AC P0A1Z0; Q60002;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Inducible lysine decarboxylase;
DE Short=LDC;
DE EC=4.1.1.18;
GN Name=cadA; Synonyms=ldcI; OrderedLocusNames=STM2559;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8736539; DOI=10.1046/j.1365-2958.1996.5441070.x;
RA Park Y.K., Bearson B., Bang S.H., Bang I.S., Foster J.W.;
RT "Internal pH crisis, lysine decarboxylase and the acid tolerance response
RT of Salmonella typhimurium.";
RL Mol. Microbiol. 20:605-611(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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 -!- 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}.
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DR EMBL; U37109; AAB41260.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21453.1; -; Genomic_DNA.
DR RefSeq; NP_461494.1; NC_003197.2.
DR RefSeq; WP_001100652.1; NC_003197.2.
DR AlphaFoldDB; P0A1Z0; -.
DR SMR; P0A1Z0; -.
DR STRING; 99287.STM2559; -.
DR PaxDb; P0A1Z0; -.
DR EnsemblBacteria; AAL21453; AAL21453; STM2559.
DR GeneID; 1254081; -.
DR KEGG; stm:STM2559; -.
DR PATRIC; fig|99287.12.peg.2700; -.
DR HOGENOM; CLU_014292_3_0_6; -.
DR OMA; NCHKSVF; -.
DR PhylomeDB; P0A1Z0; -.
DR BioCyc; SENT99287:STM2559-MON; -.
DR Proteomes; UP000001014; 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; Reference proteome.
FT CHAIN 1..714
FT /note="Inducible lysine decarboxylase"
FT /id="PRO_0000201141"
FT MOD_RES 367
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 43
FT /note="L -> V (in Ref. 1; AAB41260)"
FT /evidence="ECO:0000305"
FT CONFLICT 75..77
FT /note="EYM -> GIL (in Ref. 1; AAB41260)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="A -> R (in Ref. 1; AAB41260)"
FT /evidence="ECO:0000305"
FT CONFLICT 141..142
FT /note="RE -> PQ (in Ref. 1; AAB41260)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="N -> K (in Ref. 1; AAB41260)"
FT /evidence="ECO:0000305"
FT CONFLICT 314..315
FT /note="NT -> GA (in Ref. 1; AAB41260)"
FT /evidence="ECO:0000305"
FT CONFLICT 368..369
FT /note="LL -> MM (in Ref. 1; AAB41260)"
FT /evidence="ECO:0000305"
FT CONFLICT 421
FT /note="G -> C (in Ref. 1; AAB41260)"
FT /evidence="ECO:0000305"
FT CONFLICT 524
FT /note="I -> V (in Ref. 1; AAB41260)"
FT /evidence="ECO:0000305"
FT CONFLICT 550
FT /note="L -> PA (in Ref. 1; AAB41260)"
FT /evidence="ECO:0000305"
FT CONFLICT 585
FT /note="R -> P (in Ref. 1; AAB41260)"
FT /evidence="ECO:0000305"
FT CONFLICT 613
FT /note="L -> C (in Ref. 1; AAB41260)"
FT /evidence="ECO:0000305"
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
