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Database: UniProt
Entry: A0A024PA09_9BACI
LinkDB: A0A024PA09_9BACI
Original site: A0A024PA09_9BACI 
ID   A0A024PA09_9BACI        Unreviewed;       474 AA.
AC   A0A024PA09;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Arginine decarboxylase {ECO:0000313|EMBL:CDQ25750.1};
GN   Name=speA_2 {ECO:0000313|EMBL:CDQ25750.1};
GN   ORFNames=BN983_04113 {ECO:0000313|EMBL:CDQ25750.1};
OS   Halobacillus karajensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX   NCBI_TaxID=195088 {ECO:0000313|EMBL:CDQ25750.1, ECO:0000313|Proteomes:UP000028868};
RN   [1] {ECO:0000313|EMBL:CDQ25750.1, ECO:0000313|Proteomes:UP000028868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HD-03 {ECO:0000313|EMBL:CDQ25750.1,
RC   ECO:0000313|Proteomes:UP000028868};
RA   Urmite Genomes U.;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDQ25750.1, ECO:0000313|Proteomes:UP000028868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HD-03 {ECO:0000313|EMBL:CDQ25750.1,
RC   ECO:0000313|Proteomes:UP000028868};
RA   Khelaifia S., Croce O., Lagier J.C., Raoult D.;
RT   "Draft genome sequence of Halobacillus karajensis HK-03.";
RL   Submitted (MAY-2014) 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:CDQ25750.1}.
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DR   EMBL; CCDI010000010; CDQ25750.1; -; Genomic_DNA.
DR   RefSeq; WP_035511834.1; NZ_CCDJ010000006.1.
DR   AlphaFoldDB; A0A024PA09; -.
DR   Proteomes; UP000028868; 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: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:UP000028868}.
FT   DOMAIN          7..307
FT                   /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT                   attachment site"
FT                   /evidence="ECO:0000259|Pfam:PF01276"
FT   DOMAIN          399..449
FT                   /note="Orn/Lys/Arg decarboxylase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03711"
SQ   SEQUENCE   474 AA;  53490 MW;  44209DB52B654882 CRC64;
     MSSTNQPLYE ALKRNISKNP MSFHVPGHKY GKVYGKESMV HFQSILDIDA TEVNGLDDLH
     APEKAIREAQ ELACHFFNCD HTFFLVNGTT VGNLAMILAV CRPGNQIIVQ RNCHKSVLNG
     LELAGASPVF LSPRYEDETG RYSRVCVEDV EQVLKQYPES KAVFLTYPDY FGRVYNLEEV
     ARVVHKYNIP LLVDEAHGVH FQLEGPFPKP ALAAGADVVT QSAHKMAPAM TMASYLHIQG
     ERVDTNRIRH YLQMLQSSSP SYPLMASLDI ARSYLSSWGT EDLNLLLPYI NRVREIFSSY
     RHRWEVKLTR GHDPLKLTLD VKKGTGFEVA NIMDESGVIP EMATSSQVLL VLGLAPSVNL
     EQLEFRLRTV DYQLKKVPDR ATIREDQIPF PTIQQLELSY SDMQGRNVEK VKWVEAEGRV
     AAEALIPYPP GIPLVMKGER IGEKQIHNVQ NLIKQGARFQ NIDMKQGILV FKGE
//
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