ID   DCLY_HAFAL              Reviewed;         739 AA.
AC   P05033;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Lysine decarboxylase;
DE            Short=LDC;
DE            EC=4.1.1.18;
OS   Hafnia alvei.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Hafnia.
OX   NCBI_TaxID=569;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Fecker L.F., Beier H., Berlin J.;
RT   "Cloning and characterization of a lysine decarboxylase gene from Hafnia
RT   alvei.";
RL   Mol. Gen. Genet. 203:177-184(1986).
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   -!- 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; X03774; CAA27400.1; -; Genomic_DNA.
DR   PIR; A26016; A26016.
DR   AlphaFoldDB; P05033; -.
DR   SMR; P05033; -.
DR   STRING; 569.A6V27_04775; -.
DR   BindingDB; P05033; -.
DR   ChEMBL; CHEMBL4630867; -.
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..739
FT                   /note="Lysine decarboxylase"
FT                   /id="PRO_0000201143"
FT   REGION          714..739
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         367
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   739 AA;  83127 MW;  7E391433E6CADB50 CRC64;
     MNIIAIMNDL SAYFKEEPLR ELHQELEKEG FRIAYPKDRN DLLKLIENNS RLCGVIFDWD
     KYNLELSAEI SELNKLLPIY AFANTYSTLD VNMSDLRLNV RFFEYALGSA QDIATKIRQS
     TDQYIDTILP PLTKALFKYV KEEKYTVCTP GHMGGTAFDK SPVGSLFYDF FGENTMRSDI
     SISVSELGSL LDHSGPHRDA EEYIARTFNA DRSYIVTNGT STANKIVGMY SSPAGATILI
     DRNCHKSLTH LMMMSNVVPV YLRPTRNAYG ILGGIPQSEF TRASIEEKVK NTPNATWPVH
     AVVTNSTYDG LFYNTEYIKN TLDVKSIHFD SAWVPYTNFH PIYQGKAGMS GERVPGKIIY
     ETQSTHKLLA AFSQASMIHV KGEINEETFN EAYMMHTSTS PHYGIVASTE TAAAMMKGNA
     GKRLINGSIE RAIRFRKEIR RLRTESDGWF FDVWQPDNID EVACWPLNPR NEWHGFPNID
     NDHMYLDPIK VTLLTPGLSP NGTLEEEGIP ASIVSKYLDE HGIIVEKTGP YNLLFLFSIG
     IDKTKALSLL RALTDFKRVY DLNLRVKNVL PSLYNEAPDF YKEMRIQELA QGIHALVKHH
     NLPDLMYRAF EVLPKLVMTP HDAFQEEVRG NIEPCALDDM LGKVSANMIL PYPPGVPVVM
     PGEMLTKESR PVLSFLQMLC EIGAHYPGFE TDIHGVHRDG ATGKYMVVVL KQGADEPGDK
     PSDTVKKAPG KKPSAAKKS