ID   A0A084A4B6_9GAMM        Unreviewed;       714 AA.
AC   A0A084A4B6;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Lysine decarboxylase, constitutive {ECO:0000313|EMBL:KEY60145.1};
DE            EC=4.1.1.18 {ECO:0000313|EMBL:KEY60145.1};
GN   Name=ldcC {ECO:0000313|EMBL:KEY60145.1};
GN   ORFNames=SRDD_08950 {ECO:0000313|EMBL:KEY60145.1};
OS   Serratia sp. DD3.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=1410619 {ECO:0000313|EMBL:KEY60145.1, ECO:0000313|Proteomes:UP000017810};
RN   [1] {ECO:0000313|EMBL:KEY60145.1, ECO:0000313|Proteomes:UP000017810}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DD3 {ECO:0000313|EMBL:KEY60145.1,
RC   ECO:0000313|Proteomes:UP000017810};
RX   PubMed=25212623;
RA   Poehlein A., Freese H.M., Daniel R., Simeonova D.D.;
RT   "Draft Genome Sequence of Serratia sp. Strain DD3, Isolated from the Guts
RT   of Daphnia magna.";
RL   Genome Announc. 2:e00903-14(2014).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KEY60145.1}.
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DR   EMBL; AYKS02000031; KEY60145.1; -; Genomic_DNA.
DR   RefSeq; WP_023489820.1; NZ_AYKS02000031.1.
DR   AlphaFoldDB; A0A084A4B6; -.
DR   STRING; 1410619.SRDD_08950; -.
DR   eggNOG; COG1982; Bacteria.
DR   OrthoDB; 9761189at2; -.
DR   Proteomes; UP000017810; Unassembled WGS sequence.
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:KEY60145.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR009393-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017810}.
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   714 AA;  80530 MW;  4D8CC217471B09A3 CRC64;
     MNIIAIMSPM GVYYKDEPIR ELHTALAAMG FQLVYPKNSG DLLKLIEDNA RICGVIFDWD
     DYSLELCSEI NDLNEYLPLY AFINTHSTFD VTLHEMRMVL YFFEYGLSTA DDIAQRIRQY
     TDEYIDTITP PLTKALFTYV KEGKYTFCTP GHMGGTAFQK SPVGSLFYDF FGANTLKADI
     SVSVTELGSL LDHSGPHLEA EEYIARTFNA EQSYLVTNGT STANKIVGMY AIPAGRTVLI
     DRNCHKSLCH LLMMCDIVPI YLRPLRNAYG ILGGIPQREF THDSIAKRVA ETTNASWPVH
     AVITNSTYDG LLYNTDYIKQ TLDVASIHFD SAWVPYTNFH PIYAGKSGMS GERIPGKVIY
     ETQSTHKLLA AFSQASMIHI KGDYDEGTFN EAYMMHTTTS PHYGIVASME TAAAMLRGNP
     GRRIINRSVE RALHFRREIQ RLRDESDSWF FDIWQPGKID EAECWPLDPD DNWHGFGHTD
     ADHMYLDPIK VTILTPGMNE LGELEDSGIP AALVAKYLDQ RGIVVEKTGP YNLLFLFSIG
     IDKTKAMSLL RSLTDFKRGY DLNLLIKNML PDLYAEDPDF YRNMRIQDLA AGIHQLICKH
     NLPHLMLCAF DVLPEMKLTP YQMFQQQVSG NVETCEIDHL IGRVAANMIL PYPPGVPLVM
     PGEMITEESR GVLDFLLMLC SIGEHYPGFE TDIHGAKLTE DGRYLVNVLK TTAV
//