ID A0A0J6XC35_9ACTN Unreviewed; 495 AA.
AC A0A0J6XC35;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Ornithine decarboxylase {ECO:0000313|EMBL:KMO93475.1};
GN ORFNames=ACS04_34910 {ECO:0000313|EMBL:KMO93475.1};
OS Streptomyces roseus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=66430 {ECO:0000313|EMBL:KMO93475.1, ECO:0000313|Proteomes:UP000035932};
RN [1] {ECO:0000313|EMBL:KMO93475.1, ECO:0000313|Proteomes:UP000035932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31245 {ECO:0000313|EMBL:KMO93475.1,
RC ECO:0000313|Proteomes:UP000035932};
RA Cruz-Morales P., Martinez-Guerrero C., Morales-Escalante M.A.,
RA Yanez-Guerra L.A., Kopp J.F., Feldmann J., Ramos-Aboites H.E.,
RA Barona-Gomez F.;
RT "Recapitulation of the evolution of biosynthetic gene clusters reveals
RT hidden chemical diversity on bacterial genomes.";
RL Submitted (JUN-2015) 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}.
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:KMO93475.1}.
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DR EMBL; LFML01000163; KMO93475.1; -; Genomic_DNA.
DR RefSeq; WP_048480863.1; NZ_LFML01000163.1.
DR AlphaFoldDB; A0A0J6XC35; -.
DR STRING; 66430.ACS04_34910; -.
DR PATRIC; fig|66430.4.peg.1746; -.
DR OrthoDB; 9815233at2; -.
DR Proteomes; UP000035932; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:UniProt.
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:UP000035932}.
FT DOMAIN 6..304
FT /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT attachment site"
FT /evidence="ECO:0000259|Pfam:PF01276"
FT DOMAIN 418..466
FT /note="Orn/Lys/Arg decarboxylase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03711"
SQ SEQUENCE 495 AA; 53008 MW; F51F0E42DEFB57CE CRC64;
MDQSKTPVLD ALAAYHDTGQ TPFTPPGHKQ GRGADPRVKA ALGDAVFRSD VLATSGLDDR
TASQGVIEEA QALMAEAVGA DHAFFSTCGS SLSVKSAMLS VAGPHEELLV GRDAHKSVVS
GLILSGIRPV WVDPQWDAER HLAHPPSAEA FEAAFAAYPD ARGALVTTPT PYGTCSDLTA
IAEVCHARGK PLVVDEAWGA HLPFHPGLPT WAMDAGADVC VTSVHKMGSG LEQSSVFHLQ
GDLVKPEVLK SREDLLGTTS PSVLVYAALD GWRRQMVEQG KALYDDALDL ARLLREQIAR
IDGMRVHGRE DFCGPGKAAD ADPLQIIIDI SAWNVPGYRA ADWLRRHHRV NLHLADHRRI
SAQLTHADDE RSARVLLTAL TDLAAHVPEL RTGQPVEVPA PARLRLEQAA LPRDAFFGPT
EQVPWQKAAG RIAAEMLTPY PPGIPAALPG ERLTDDVLCY LRSGVEAGMI IPDAVDPQVN
SVRVSIESGR SGTGT
//
