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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//