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Database: UniProt
Entry: A0A1V4EX92_9BACL
LinkDB: A0A1V4EX92_9BACL
Original site: A0A1V4EX92_9BACL 
ID   A0A1V4EX92_9BACL        Unreviewed;       484 AA.
AC   A0A1V4EX92;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Arginine decarboxylase {ECO:0000313|EMBL:OPG17553.1};
GN   ORFNames=B2M26_00900 {ECO:0000313|EMBL:OPG17553.1};
OS   Ferroacidibacillus organovorans.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC   Ferroacidibacillus.
OX   NCBI_TaxID=1765683 {ECO:0000313|EMBL:OPG17553.1, ECO:0000313|Proteomes:UP000190229};
RN   [1] {ECO:0000313|EMBL:OPG17553.1, ECO:0000313|Proteomes:UP000190229}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Huett2 {ECO:0000313|EMBL:OPG17553.1,
RC   ECO:0000313|Proteomes:UP000190229};
RA   Schopf S.;
RT   "Draft genome of Acidibacillus ferrooxidans Huett2.";
RL   Submitted (FEB-2017) 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:OPG17553.1}.
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DR   EMBL; MWPS01000002; OPG17553.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V4EX92; -.
DR   Proteomes; UP000190229; Unassembled WGS sequence.
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.
DR   PROSITE; PS00703; OKR_DC_1; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190229}.
FT   DOMAIN          222..236
FT                   /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT                   attachment site"
FT                   /evidence="ECO:0000259|PROSITE:PS00703"
SQ   SEQUENCE   484 AA;  52699 MW;  032C4FA9EB44B1BB CRC64;
     MSNQQDTPLF TALRKHAERQ PLQFHIPGHK TGLAMDPEFR DFMGQNALSI DLINIGPLDD
     LMHPTGIIAE AQALAAEAFG ADATYFSVQG TSGAIMAMIL SVVGPGDEIL VPRNIHKSVL
     SAIILSGARP FFLQPEVDLH LGIAHGLRLE TVIAGLDTHP NAKAVLVINP TYFGVATDLR
     SIVHVAHARG VLVLVDEAHG VHTYFHEALP DSAMQAGCDL SATSVHKLGG SLTQSSVLNV
     REGLVRARHV HSILSMLHTT STSYLLLASL DAARRQLAVH GRGRIANAIT LAEDARLRIN
     EIEGLYCFGR EILQSSATFA FDPLKLTIRV ADIGISGYEV EGILRDHYNI EVEMSDLYNI
     LCIISFGDTE SSVAQLIHAL RDLVEIERLR THVPRKIVVP STPRLAMPPR DAFYADSEVV
     TLREAIGRTI ADMIMVYPPG IPILLPGEIV TLDNVQYIEE NLAEGLPVQG PDDPSIQTVR
     VVRE
//
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