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 03-MAY-2023, entry version 92.
DE RecName: Full=Lysine decarboxylase;
DE Short=LDC;
DE EC=4.1.1.18;
OS Hafnia alvei.
OC Bacteria; Pseudomonadota; 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: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 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
//
