ID A0A150WJD6_BDEBC Unreviewed; 750 AA.
AC A0A150WJD6;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Lysine decarboxylase {ECO:0000313|EMBL:KYG63810.1};
GN ORFNames=AZI86_13390 {ECO:0000313|EMBL:KYG63810.1};
OS Bdellovibrio bacteriovorus.
OC Bacteria; Bdellovibrionota; Bdellovibrionia; Bdellovibrionales;
OC Pseudobdellovibrionaceae; Bdellovibrio.
OX NCBI_TaxID=959 {ECO:0000313|EMBL:KYG63810.1, ECO:0000313|Proteomes:UP000075320};
RN [1] {ECO:0000313|EMBL:KYG63810.1, ECO:0000313|Proteomes:UP000075320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R0 {ECO:0000313|EMBL:KYG63810.1,
RC ECO:0000313|Proteomes:UP000075320};
RA Ploux O.;
RL Submitted (MAR-2016) 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:KYG63810.1}.
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DR EMBL; LUKE01000003; KYG63810.1; -; Genomic_DNA.
DR RefSeq; WP_061835704.1; NZ_LUKE01000003.1.
DR AlphaFoldDB; A0A150WJD6; -.
DR Proteomes; UP000075320; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000075320}.
FT DOMAIN 391..405
FT /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT attachment site"
FT /evidence="ECO:0000259|PROSITE:PS00703"
FT MOD_RES 396
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR009393-1"
SQ SEQUENCE 750 AA; 84619 MW; 36F3CC685CDD4FB8 CRC64;
MKFKFPVVII DEDFRSENAS GSGIRALAAA IESEGMEVLG VTSYGDLTAF AQQQSRASAF
LLSIDDEEFG GGSQNEIAEA LKGVRAFIEE IRFKNAEIPI YLYGETRTSR HIPNDILREL
HGFIHMHEDT PEFVAKHIIR EAKSYLDSIA PPFFRALLNY AQNGSYSWHC PGHSGGVAFL
KSPVGQMFHQ FFGENMLRAD VCNAVDELGQ LLDHTGPVAA SERNAARIFN ADHLFFVTNG
TSTSNKIVWH STVGPDDIVV VDRNCHKSNL HAIMMTGAIP VFLTPTRNHY GIIGPIPKQE
FSMESIQRKI DANPFIKDKT KKPRILTITQ STYDGVVYNV ETIKEMLDGK IHTLHFDEAW
LPHAAFHDFY KDMHAIGKDR PRAKDSIIFS TQSTHKLLAG LSQASQILVS ESENKKLNHH
IFNEAYLMHT STSPQYSIIA SCDVAASMME APGGTALVEE SIAEAMDFRR AMKKVDDEWG
TDWWFKVWGP EDITEEGVGS RENWVLKPED KWHGFGNLAE GFNMLDPIKA TIITPGLDVD
GDFADQGIPA AMVTKYLAEH GVIVEKCGLY SFFIMFTIGI TKGRWNTLLT ALQQFKDDYD
KNQPLWKILP QFVAAHPRYE RMGLRDLCQQ IHEAYKFKNV ARMTTEMYLS EMQPAMKPSD
AFAKMAHEEI ERIEIDDLEN RVTAVLLTPY PPGIPLLIPG ERFNKTVVDY LKFAREFNLK
FPGFETDVHG LVAERDENGK KRYFVDCIKN
//
