ID A0A427CBK7_9GAMM Unreviewed; 762 AA.
AC A0A427CBK7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 11.
DE SubName: Full=Lysine decarboxylase {ECO:0000313|EMBL:RRU14296.1};
GN ORFNames=EGJ34_10705 {ECO:0000313|EMBL:RRU14296.1};
OS Stenotrophomonas sp. 278.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=2479851 {ECO:0000313|EMBL:RRU14296.1, ECO:0000313|Proteomes:UP000274083};
RN [1] {ECO:0000313|EMBL:RRU14296.1, ECO:0000313|Proteomes:UP000274083}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=278 {ECO:0000313|EMBL:RRU14296.1,
RC ECO:0000313|Proteomes:UP000274083};
RA D'Souza A.W., Potter R.F., Wallace M., Shupe A., Patel S., Sun S., Gul D.,
RA Kwon J.H., Andleeb S., Burnham C.-A.D., Dantas G.;
RT "Transmission dynamics of multidrug resistant bacteria on intensive care
RT unit surfaces.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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:RRU14296.1}.
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DR EMBL; RHPP01000053; RRU14296.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A427CBK7; -.
DR OrthoDB; 9761189at2; -.
DR Proteomes; UP000274083; 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 390..404
FT /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT attachment site"
FT /evidence="ECO:0000259|PROSITE:PS00703"
FT MOD_RES 395
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR009393-1"
SQ SEQUENCE 762 AA; 84847 MW; FAEF9DECA44EA6EE CRC64;
MYFKSLDYPV IVIDADYESP RIGGILIRAL VEELRRNEQR VLCGLTLADA QAGARTYVAA
SAVLISIDGT EDEPTEFQRL LGFLREQSAR RGGLPVFLYG ERRTIEKVPS KLLKYVHGYI
FLFEDTKSFI ARQVMRAAED YMHTLLPPFF KALIHHAAES NYSWHTPGHA GGVAFTKSPV
GRAFHQFYGE NTLRSDLSIS VPELGSLLDH SGPIKEAENE AARDFGADHT FFVTNGTSTA
NKIVWHGTVG RGDVVFVDRN CHKSLLHALI MTGGVPVYFT PSRNAHGIIG PISLDQFTPE
ALQQAIAANP LARQAYQAGS KPRIAVVTNS TYDGLCYNAE KIADEIGTAV DFLHFDEAWY
AYAAFHPFYE NHYGMAKGKP REQDAIIFTT HSTHKLLAAF SQASMIHVRN AATRELDAER
FNEAFMMHTT TSPHYGVIAA CDVASKMMEG AAGESLVQEM HDEAIAFRRA MLHVRDDLGR
DDWWFSVWQP DKLERSLAKG DAPAPLVAKR EEWYLQPEAY WHGFDGLVED YVLIDPIKVT
LLTPGLSING EVAERGIPAA VLSKFLWTRG ITVEKTNLYS VLFLFSMGIT KGKWSTLVTE
LMAFKELYDS NAPLSRALPD LAADYGDIYA GWGLRDLCQA LHDFNRGFEV AKVMREMYVD
LPTPVMTPAQ AYDHLVRGEI ERVDIEALSG RVAGTMLVPY PPGIPTIMPG ERFGSSDEPI
IQSLRIAREQ NARFPGFESD VHGLIIDRSG EAPSYKVEVL KV
//