ID I7J216_9BURK Unreviewed; 752 AA.
AC I7J216;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Probable orn/arg/lys decarboxylase {ECO:0000313|EMBL:CCG19863.1};
DE EC=4.1.1.19 {ECO:0000313|EMBL:CCG19863.1};
GN ORFNames=KUM_1079 {ECO:0000313|EMBL:CCG19863.1};
OS Taylorella asinigenitalis 14/45.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Taylorella.
OX NCBI_TaxID=1091495 {ECO:0000313|EMBL:CCG19863.1};
RN [1] {ECO:0000313|EMBL:CCG19863.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=14/45 {ECO:0000313|EMBL:CCG19863.1};
RX PubMed=22541164; DOI=10.1016/j.vetmic.2012.03.041;
RA Hauser H., Richter D.C., van Tonder A., Clark L., Preston A.;
RT "Comparative genomic analyses of the Taylorellae.";
RL Vet. Microbiol. 159:195-203(2012).
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-I family.
CC {ECO:0000256|ARBA:ARBA00010671}.
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DR EMBL; HE681424; CCG19863.1; -; Genomic_DNA.
DR AlphaFoldDB; I7J216; -.
DR KEGG; tat:KUM_1079; -.
DR HOGENOM; CLU_014292_3_0_4; -.
DR BioCyc; TASI1091495:G13GE-1072-MONOMER; -.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0008792; F:arginine decarboxylase activity; IEA:UniProtKB-EC.
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 Lyase {ECO:0000313|EMBL:CCG19863.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR009393-1}.
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 752 AA; 85520 MW; FD08C7F7F2BC6B60 CRC64;
MKFRFPIVII DEDFRSDSAS GFGIRALADA IEAEGFEVLP ATSYGDLTSF VQQQSRASAF
ILSIDDEEFE SDSPQDVAEA IRNLRSFINE LRFRNEDIPI YLHGETRTSE HIPNDILKEL
HGFIHMFEDT PEFVARHIVH EAKSYLDTLA PPFFRELVNY AHDGSYSWHC PGHSGGVAFL
KSPVGQMFHQ FFGENMLRAD VCNAVEELGQ LLDHTGPIAK SEINAARIFN ADHCYFVTNG
TSTSNKIVWH GNVAENDIVV VDRNCHKSIL HAITMTGAIP VFLKPTRNNL GIIGPIPLSE
FEPENIKKKI ADNPFISEEL KKKPRILTLT QGTYDGILYN VEMIKEKLGD TMENLHFDEA
WLPHAAFHEF YENMHAIGRG RPRSKESIIY ATHSTHKMLA GISQASQIIV QDSESRKLDR
NIFNEAFLMH TSTSPQYAII ASCDVAAAMM EPPGGTALVE ESLRESMDFR RAMRKVASEF
GKDDWWFKVW GPPRLVQEDI GWQGDWLLEP DAEWHGFSNI TDGFTMLDPI KTTIVTPGLE
IDGTFDETGI PASLVSKYLT EHGIVVEKTG LYSFFIMFTI GITKGRWNTL LTSLQQFKDD
YDKNQPLWRS MPDFIKQYPK YEAYGLRDLC QELHEAYRKR DLARITTEVY LSDMESAMKP
KDAHNKMTRR EIERVNIDDL EGRVTAVLLT PYPPGIPLLI PGERFNKTIV QYLKFVCEFN
VEFPGFETMV HGLGSEVLPK GEIHYYVDCL MD
//
