ID A7G9F8_CLOBL Unreviewed; 482 AA.
AC A7G9F8;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 24-JAN-2024, entry version 68.
DE SubName: Full=Orn/Lys/Arg decarboxylase {ECO:0000313|EMBL:ABS41746.1};
GN OrderedLocusNames=CLI_0110 {ECO:0000313|EMBL:ABS41746.1};
OS Clostridium botulinum (strain Langeland / NCTC 10281 / Type F).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=441772 {ECO:0000313|EMBL:ABS41746.1, ECO:0000313|Proteomes:UP000002410};
RN [1] {ECO:0000313|Proteomes:UP000002410}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Langeland / NCTC 10281 / Type F
RC {ECO:0000313|Proteomes:UP000002410};
RA Brinkac L.M., Daugherty S., Dodson R.J., Madupu R., Brown J.L., Bruce D.,
RA Detter C., Munk C., Smith L.A., Smith T.J., White O., Brettin T.S.;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP000728; ABS41746.1; -; Genomic_DNA.
DR RefSeq; WP_011987181.1; NC_009699.1.
DR AlphaFoldDB; A7G9F8; -.
DR KEGG; cbf:CLI_0110; -.
DR HOGENOM; CLU_025925_2_1_9; -.
DR OMA; NCHKSVF; -.
DR Proteomes; UP000002410; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR CDD; cd00615; Orn_deC_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.90.105.10; Molybdopterin biosynthesis moea protein, domain 2; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR000310; Orn/Lys/Arg_deCO2ase_major_dom.
DR InterPro; IPR008286; Prn/Lys/Arg_de-COase_C.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43277; ARGININE DECARBOXYLASE; 1.
DR PANTHER; PTHR43277:SF4; ARGININE DECARBOXYLASE; 1.
DR Pfam; PF01276; OKR_DC_1; 1.
DR Pfam; PF03711; OKR_DC_1_C; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}.
FT DOMAIN 5..368
FT /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT attachment site"
FT /evidence="ECO:0000259|Pfam:PF01276"
FT DOMAIN 370..458
FT /note="Orn/Lys/Arg decarboxylase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03711"
SQ SEQUENCE 482 AA; 55797 MW; 054939CCF41CA01C CRC64;
MGELPILNGV LKYIKEKNIL FSMPGHKGSL GFLFTEEGKK FCENIPQCDL TEVEGLDNLH
NSEGIIKESG YLLSRFYNSK KSYFLVNGST SGNLAMIFSC FKEEDKIIVE RNCHRSIFNG
IIMRKLKPIY IKNKVYRQFN APLSIDLEHF LSLIKENKDA KGIVITYPNY YGVCPNLKII
IKEAKKYNMK VLIDSAHGAH FGVCEKLPES ALELGADMVV MSAHKTLPSL TQTAFLHIGK
DSIIDINKVD FYISAFSSTS PSYLFLCSMD YSRFYLEKYG QEHYNELINR ANYYRKKINL
LDSFYVLNHS DIKHLNLKYK DVMDIDLTRY TINIKNGLNA SCLSKYLREC GIQCEMSDGN
NIILILSPFY NEDVMDRLYE SLYEWDKNYN KDKYNYNINY NYIETNMNMY PYEVLEKEYL
WIDYKDSLGK ISYNNIVPYP PGVPIIMAGE IINKEIIDAI CYYKNNGIDV LGLNNNKIQI
VK
//