ID A0A1B2QYC1_9BORD Unreviewed; 756 AA.
AC A0A1B2QYC1;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Lysine decarboxylase {ECO:0000313|EMBL:AOB29757.1};
GN ORFNames=AKI39_02240 {ECO:0000313|EMBL:AOB29757.1};
OS Bordetella sp. H567.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=1697043 {ECO:0000313|EMBL:AOB29757.1, ECO:0000313|Proteomes:UP000093512};
RN [1] {ECO:0000313|Proteomes:UP000093512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H567 {ECO:0000313|Proteomes:UP000093512};
RA Babu N.S., Beckwith C.J., Beseler K.G., Brison A., Carone J.V.,
RA Caskin T.P., Diamond M., Durham M.E., Foxe J.M., Go M., Henderson B.A.,
RA Jones I.B., McGettigan J.A., Micheletti S.J., Nasrallah M.E., Ortiz D.,
RA Piller C.R., Privatt S.R., Schneider S.L., Sharp S., Smith T.C.,
RA Stanton J.D., Ullery H.E., Wilson R.J., Serrano M.G., Buck G., Lee V.,
RA Wang Y., Carvalho R., Voegtly L., Shi R., Duckworth R., Johnson A.,
RA Loviza R., Walstead R., Shah Z., Kiflezghi M., Wade K., Ball S.L.,
RA Bradley K.W., Asai D.J., Bowman C.A., Russell D.A., Pope W.H.,
RA Jacobs-Sera D., Hendrix R.W., Hatfull G.F.;
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-I family.
CC {ECO:0000256|ARBA:ARBA00010671}.
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DR EMBL; CP012334; AOB29757.1; -; Genomic_DNA.
DR RefSeq; WP_066632034.1; NZ_CP012334.1.
DR AlphaFoldDB; A0A1B2QYC1; -.
DR STRING; 1697043.AKI39_02240; -.
DR KEGG; boh:AKI39_02240; -.
DR PATRIC; fig|1697043.4.peg.461; -.
DR OrthoDB; 9761189at2; -.
DR Proteomes; UP000093512; Chromosome.
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:UP000093512}.
FT DOMAIN 392..406
FT /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT attachment site"
FT /evidence="ECO:0000259|PROSITE:PS00703"
FT MOD_RES 397
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR009393-1"
SQ SEQUENCE 756 AA; 85361 MW; C9146EDE1CDC43CC CRC64;
MKFRFPIVII DEDYRSENAS GLGIRALASA IEAEGVEVLG VTSYGDLSSF AQQQSRASAF
ILSIDDEEFD VDSPEDVASA IKNLRTFIGE LRFRNADIPI YLYGETRTSQ HIPNDILREL
HGFIHMFEDT PEFVARHIIR EARAYVDGLP PPFFRELVKY AQDGSYSWHC PGHSGGVAFL
KSPVGQMFHQ FFGENMLRAD VCNAVDELGQ LLDHTGPVAE SELNAARIFH ADHCYFVTNG
TSTSNKVVWH ANVAAGDVVV VDRNCHKSIL HAITMTGAIP VFLRPTRNHL GIIGPIPIEE
FEPESILKKI EANPFAREAK DKKPRILTLT QSTYDGVIYN VEMIKAKLGD YVDTLHFDEA
WLPHAAFHEF YQDMHAIGQG RPRSDSAMVF ATHSTHKLLA GISQASQIIV QESKTRKLDR
NIFNEAYLMH TSTSPQYAII ASCDVAAAMM EPPGGTALVE ESIREAMDFR RAMRKVESEF
GRNDWWFKVW GPNRLVSDGI GNRDEWLLES GDHWHGFGDI ADGFNMLDPI KATIITPGLD
ISGSFGETGI PAALVSKYLT EHGVVVEKTG LYSFFILFTI GITKGRWNTL LTALQQFKDD
YDRNQPMWRI LPEFCRDHRQ YERIGLRDLC QQIHEAYRES DVARLTTEMY LSDMVPALKP
SDAFARMAHR QVERVAIENL EGRVTGVLLT PYPPGIPLLI PGERFNRTIV QYLQFARAFN
ERFPGFETDI HGLAEDVDDD GQVRYYVDCL KEEQTR
//
