ID A0A2G0Q8V4_9GAMM Unreviewed; 738 AA.
AC A0A2G0Q8V4;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Lysine decarboxylase, inducable {ECO:0000313|EMBL:PHM55660.1};
GN ORFNames=Xhom_02408 {ECO:0000313|EMBL:PHM55660.1};
OS Xenorhabdus hominickii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=351679 {ECO:0000313|EMBL:PHM55660.1, ECO:0000313|Proteomes:UP000225433};
RN [1] {ECO:0000313|EMBL:PHM55660.1, ECO:0000313|Proteomes:UP000225433}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17903 {ECO:0000313|EMBL:PHM55660.1,
RC ECO:0000313|Proteomes:UP000225433};
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:PHM55660.1}.
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DR EMBL; NJAI01000003; PHM55660.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G0Q8V4; -.
DR STRING; 351679.A9255_11250; -.
DR Proteomes; UP000225433; 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; 3.40.50.220; -; 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; IPR011006; CheY-like_superfamily.
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; IPR027464; Ornithine_deCO2ase_N.
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; CONSTITUTIVE ORNITHINE DECARBOXYLASE; 1.
DR PANTHER; PTHR45229:SF1; INDUCIBLE 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; SSF52172; CheY-like; 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 351..365
FT /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT attachment site"
FT /evidence="ECO:0000259|PROSITE:PS00703"
FT MOD_RES 356
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR009393-1"
SQ SEQUENCE 738 AA; 83876 MW; FEEBA787A9A1D35B CRC64;
MIKKFNIACS NNTCDIFNSE RETINIKETH FIDVSAIVIS LEDALNGELE RIEETQYPIP
IYLVLPKNET LPVRLLSRIT GVFQSEKGHE NFYGQQLDTT AEKYEKSLLP PFFGAMTEYV
AQGNIAFDCP GHQGGQFFRN HPCGIQFFNY FGETLFRSDL CNADVYMGDL LIHEGAPCDA
QKNAAKIFNA DKTYFVLNGT SSSNRVVLNA LLTPGDLVLF DRNNHKSNHV GALIQSGATP
IYLETTRNLF GLIGGIDSHC FEEAYLRNLI QEVAPERTTE KRPFRLAVIQ LVTYDGVVYN
AKQVVDKIGH LCDYILFDSA WLGYEQFIPM MADGSPLLLD LNENDPGIIV TQSVHKQQAG
LSQSSQIHKK DRHIKGQSRY VNHKRFNNSF TAHASTSPFY PLFAALDVNA KMHEGQNGKK
MWMDCVKMSI EARKLILQQC KYIKPFISDN VDGRHWADYE TDEIANDLRF FYFIPGEKWH
SFDGYSEQQY FVDPCKLLLI TPGVNANTGE YDKFGVPATV LAYFLRENSI IPEKYALNSI
LFLLTPAGNT AKIGYLVSQL IHFEQLLEQD APLETVLPSL CRNYPERYRG QTIRQLCQEM
HSLAINRNIK QLQKEIFRKS HFPKIAMPPQ KANIELVRGN VELVALRDIE GLIAADGAVP
YPPGVCCIVP GEIWGDSVLR YFLALEENIN QFPGFEQELQ GVYLQKEEDG YTRIYGYIIK
SDDYNPQRSN LKDKEDKK
//
