ID   A0A1I7KRP5_9BACL        Unreviewed;       491 AA.
AC   A0A1I7KRP5;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Arginine/lysine/ornithine decarboxylase {ECO:0000313|EMBL:SFV00085.1};
GN   ORFNames=SAMN05421543_11859 {ECO:0000313|EMBL:SFV00085.1};
OS   Alicyclobacillus macrosporangiidus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC   Alicyclobacillus.
OX   NCBI_TaxID=392015 {ECO:0000313|EMBL:SFV00085.1, ECO:0000313|Proteomes:UP000183508};
RN   [1] {ECO:0000313|Proteomes:UP000183508}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17980 {ECO:0000313|Proteomes:UP000183508};
RA   Varghese N.;
RL   Submitted (OCT-2016) 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; FPBV01000018; SFV00085.1; -; Genomic_DNA.
DR   RefSeq; WP_074954791.1; NZ_FPBV01000018.1.
DR   AlphaFoldDB; A0A1I7KRP5; -.
DR   STRING; 392015.SAMN05421543_11859; -.
DR   OrthoDB; 9815233at2; -.
DR   Proteomes; UP000183508; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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; 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:UP000183508}.
FT   DOMAIN          19..295
FT                   /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT                   attachment site"
FT                   /evidence="ECO:0000259|Pfam:PF01276"
FT   DOMAIN          417..451
FT                   /note="Orn/Lys/Arg decarboxylase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03711"
SQ   SEQUENCE   491 AA;  50650 MW;  0317E1F550C87AE6 CRC64;
     MTGTVDTDGK PGWDEAEAPI LAALVRTAGR IRLPLFVPGH KQGRLLPGVL SSWLGAAAKI
     DLTELPGLDN LHRAEGCILR SEALAAAHYG AEWCLFSVNG STAGVMAALL AAAPGGKVVF
     AGPFHESAWR GLVVAGAEPV LIPGTWDAER QVVRPPAPAE VARMLADARG IRAVYVTSPT
     YAGVRAPVRE LAEVAHRHGV PLIVDEAHGA HFGLVPELPP HSIQEGADVV VQSVHKMLPG
     LTQTAWVLGQ GGRVDRAAVV EALSMLQTTS PSYLLLASLD AAQLWLRTEG ADAAARAVAA
     MDAVWQAYPH HRLDDPLRHF LPTGGMAASR RVQSALQEAG IWVEYADPLG VLSVFGLAAE
     PTGVGRYLDA LTGVAPPVAG GPAAGSAAGL ASPLVRLTAH SAAPVAAAPR EVFLAPRTWV
     PAGSAAGRVA AGLITPYPPG VPVVLPGQTL DEGLCAALSE LLETGYEVHG VDAAGRIPVM
     QEGGAAGVHH V
//