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Database: UniProt
Entry: A0A2D0LCW9_9GAMM
LinkDB: A0A2D0LCW9_9GAMM
Original site: A0A2D0LCW9_9GAMM 
ID   A0A2D0LCW9_9GAMM        Unreviewed;       762 AA.
AC   A0A2D0LCW9;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Lysine decarboxylase, inducable {ECO:0000313|EMBL:PHM73502.1};
GN   ORFNames=Xkoz_01918 {ECO:0000313|EMBL:PHM73502.1};
OS   Xenorhabdus kozodoii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=351676 {ECO:0000313|EMBL:PHM73502.1, ECO:0000313|Proteomes:UP000221101};
RN   [1] {ECO:0000313|EMBL:PHM73502.1, ECO:0000313|Proteomes:UP000221101}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17907 {ECO:0000313|EMBL:PHM73502.1,
RC   ECO:0000313|Proteomes:UP000221101};
RX   PubMed=28993611; DOI=10.1038/s41564-017-0039-9;
RA   Tobias N.J., Wolff H., Djahanschiri B., Grundmann F., Kronenwerth M.,
RA   Shi Y.M., Simonyi S., Grun P., Shapiro-Ilan D., Pidot S.J., Stinear T.P.,
RA   Ebersberger I., Bode H.B.;
RT   "Natural product diversity associated with the nematode symbionts
RT   Photorhabdus and Xenorhabdus.";
RL   Nat. Microbiol. 2:1676-1685(2017).
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:PHM73502.1}.
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DR   EMBL; NJCX01000011; PHM73502.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2D0LCW9; -.
DR   OrthoDB; 9761189at2; -.
DR   Proteomes; UP000221101; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
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   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR009393-1}.
FT   DOMAIN          383..397
FT                   /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT                   attachment site"
FT                   /evidence="ECO:0000259|PROSITE:PS00703"
FT   MOD_RES         388
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009393-1"
SQ   SEQUENCE   762 AA;  85884 MW;  D1A50117A7ADC8FC CRC64;
     MKVLIAKNEV GTRYHSHYID NAVHRLADNL IEKDVDVVIA ESFDDSYTII SANEPFDCLM
     ISCALMDDGL YLQIQKLLNK LFERQENVPV FLLSDREKTV FLLNHELLEQ LTEFAWILED
     SADFIAGRAI AAMQRYRQQL FPPLMSALMK YSRTYEYSWA APGHQGGVGF NKTPVGRFYH
     DYYGENLFRT DMGIERTSLG SLLDHSGAFG ESERNAARVF GADHSYSVVV GTSGSNRTIM
     QACMTEDDVV IIDRNCHKSI EQGLILTGAK PVYMLPSRNR YGIIGPIYPQ EMQAKTLQKK
     LKQNPLTQGM ASQKPIYSVV TNCTYDGVCY NAKRVEELLD KSVDRIHFDE AWYGYARFNP
     IYHDHYAMRG NPKNHAGATV FATHSSHKLL NALSQASFIH VRDGRNPVDF SRFNQAYMMH
     ATTSPLYAIC ASNDIAVAMM DGNSGYSLTQ EVIEEAVDFR QALARLQRDF SKKGDWFFKP
     WNQEKVTDPA TGKKMAFEDA PKELLTKEQS CWAMRPEDSW HGFDDLPDNW SMLDPIKVSI
     LAPGMGDNGK LKKHGVPAAL VTAWLGQHGI VPTRTTDFQI MFLFSMGITK GKWGTLLNTL
     LSFKQHYDAN APLSKVLPDL VDQYPAVYGD LGLKELGDKM FDYLRQNNPG EKLNQAYAGL
     PKMEMTPRAA YQAIVTNNVE MVAIDDLAHR VAANSIIPYP PGIPMLLSGE NFGDKTSPQI
     GYLHALQKWD HEFPGFEHET EGTEIISGIY HVMCIKKVKT GR
//
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