ID Q97GM8_CLOAB Unreviewed; 487 AA.
AC Q97GM8;
DT 01-OCT-2001, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2001, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE SubName: Full=Lysine decarboxylase {ECO:0000313|EMBL:AAK80294.1};
GN OrderedLocusNames=CA_C2338 {ECO:0000313|EMBL:AAK80294.1};
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562 {ECO:0000313|EMBL:AAK80294.1, ECO:0000313|Proteomes:UP000000814};
RN [1] {ECO:0000313|EMBL:AAK80294.1, ECO:0000313|Proteomes:UP000000814}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787
RC {ECO:0000313|Proteomes:UP000000814};
RX PubMed=11466286; DOI=10.1128/JB.183.16.4823-4838.2001;
RA Nolling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
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; AE001437; AAK80294.1; -; Genomic_DNA.
DR PIR; C97188; C97188.
DR RefSeq; NP_348954.1; NC_003030.1.
DR RefSeq; WP_010965635.1; NC_003030.1.
DR AlphaFoldDB; Q97GM8; -.
DR STRING; 272562.CA_C2338; -.
DR GeneID; 44998813; -.
DR KEGG; cac:CA_C2338; -.
DR PATRIC; fig|272562.8.peg.2534; -.
DR eggNOG; COG1982; Bacteria.
DR HOGENOM; CLU_025925_2_1_9; -.
DR OrthoDB; 9815233at2; -.
DR Proteomes; UP000000814; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR CDD; cd00615; Orn_deC_like; 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; 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 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; SSF55904; Ornithine decarboxylase C-terminal domain; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000000814}.
FT DOMAIN 9..373
FT /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT attachment site"
FT /evidence="ECO:0000259|Pfam:PF01276"
FT DOMAIN 406..467
FT /note="Orn/Lys/Arg decarboxylase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03711"
SQ SEQUENCE 487 AA; 53264 MW; FF9EA63F4DC02F47 CRC64;
MYKLNQNETP LFNALMEYVN RDTIPFHVPG HKKGNGIDKE FKNFIGENPF KIDVTVFKLV
DSLHHPTGPI KKAQELAADA YGSKAAFYSV NGTSGAIQGM ILSVVGDGDK IIVPRNVHKS
VTAGIILSGA VPVYMHPEVD RRVGIAHGVS PETVGETLKN NPDAKAVLLI NPTYYGVSTD
IKKIADIVHS YDIPLIVDEA HGPHLSFNDR LPVSALKAGA DMCAQSTHKI IGALTQMSLL
HVNSDRIDMN RVQQIMNLLQ TTSPSYILMA SMDCARRQIA LHGKELLDGT IDLCNYARRE
INKIPGFYCF GEEVLGKPGS YAFDPTKLTI TCTDLGITGY DLDMLLANDY HIQVELSDLY
NVLAVGSFGD TKENIDALIN ALRQISKSIS STVKNKKNSF IDIPDVPERI LSPRDAFNGA
KESMLIKDSV GKTSGEFLMA YPPGIPVLCP GEIITQEIID YVSDLKAAGL YVQGTEDPDV
NYIKVLK
//
