ID   A0A1I6BAG9_9BACI        Unreviewed;       474 AA.
AC   A0A1I6BAG9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Arginine/lysine/ornithine decarboxylase {ECO:0000313|EMBL:SFQ77931.1};
GN   ORFNames=SAMN05421670_0294 {ECO:0000313|EMBL:SFQ77931.1};
OS   Psychrobacillus psychrotolerans.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Psychrobacillus.
OX   NCBI_TaxID=126156 {ECO:0000313|EMBL:SFQ77931.1, ECO:0000313|Proteomes:UP000198734};
RN   [1] {ECO:0000313|Proteomes:UP000198734}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11706 {ECO:0000313|Proteomes:UP000198734};
RA   Varghese N., Submissions S.;
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; FOXU01000013; SFQ77931.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6BAG9; -.
DR   STRING; 126156.SAMN05421670_0294; -.
DR   Proteomes; UP000198734; 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:SF3; LYSINE 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:UP000198734}.
FT   DOMAIN          7..277
FT                   /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT                   attachment site"
FT                   /evidence="ECO:0000259|Pfam:PF01276"
FT   DOMAIN          387..450
FT                   /note="Orn/Lys/Arg decarboxylase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03711"
SQ   SEQUENCE   474 AA;  54503 MW;  9A46EE4D19C459D9 CRC64;
     MMQEKRPLVE ALEQFHKKKS ISFHVPGHKH GLLSNLPQLI SNSMQYDLTE LDGLDDYHHP
     KEAIKEAEEL LTRLYNTDDS FFLVNGTTIG NIAMIYATCQ YGEQIIVQRN AHKSIFHAIE
     LVGAEPIYVS PIWDEHSKTA SYVPLEVIEE AIQQYPFAKA VVLTYPNYYG VCSRDLEEII
     NLCHSLEMPV LVDEAHGAHF QSHKEFPKSA LLYGADVVVQ SAHKTLPSLT MGSYIHIRSH
     LIESKRVNKY LRMLQSSSPS YLILASLDDA RSYVERYSPM DYKQLLDRRE VFIDALETIP
     LIEVVQVDDP LKLLIRVEKY SGFQVQQAFE KQNIYVELAD IYQVLLILPL LKVEHEFPFA
     EIRKRMKYAV EDLKKETPEY TSSTLYMQQK NISTLQMHLE LVNEKQGEWI PYARSIGRIA
     KGMIVPYPPG IPLLLPGEKI TVPILTELEV WIEKGASFQG EHQLEEKLIY VVEE
//