ID   A0A268EAF7_9BACI        Unreviewed;       491 AA.
AC   A0A268EAF7;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 11.
DE   SubName: Full=Arginine decarboxylase {ECO:0000313|EMBL:PAD70116.1};
GN   ORFNames=CHH83_04980 {ECO:0000313|EMBL:PAD70116.1};
OS   Bacillus sp. 7586-K.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=2021690 {ECO:0000313|EMBL:PAD70116.1, ECO:0000313|Proteomes:UP000216230};
RN   [1] {ECO:0000313|EMBL:PAD70116.1, ECO:0000313|Proteomes:UP000216230}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=7586-K {ECO:0000313|EMBL:PAD70116.1,
RC   ECO:0000313|Proteomes:UP000216230};
RA   Kalinowski J., Ahrens B., Al-Dilaimi A., Winkler A., Wibberg D.,
RA   Schleenbecker U., Ruckert C., Wolfel R., Grass G.;
RT   "Isolation and whole genome analysis of endospore-forming bacteria from
RT   heroin.";
RL   Submitted (JUL-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:PAD70116.1}.
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DR   EMBL; NPCL01000014; PAD70116.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A268EAF7; -.
DR   OrthoDB; 9815233at2; -.
DR   Proteomes; UP000216230; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   CDD; cd00615; Orn_deC_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
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   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
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:UP000216230}.
FT   DOMAIN          221..235
FT                   /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT                   attachment site"
FT                   /evidence="ECO:0000259|PROSITE:PS00703"
SQ   SEQUENCE   491 AA;  53831 MW;  CCF659E885A6F7E8 CRC64;
     MSQNETPLFT GLVEHAKKNP IQFHIPGHKK GAGIEPEFRQ FIGENALSID LINIGPLDDL
     HAPKGIIKKA QELAAEAFGA DYTYFSVQGT SGAIMTMVMA VCGPGDKIIV PRNVHKSIMS
     AIVFSGAIPI FIHPEIDKEL GISHGITIDA VAKALEQNPD AKGVLVINPT YFGISADLKK
     IVEIAHSYNV PVLVDEAHGV HIHFHEDLPM SAMQAGADIA ATSVHKLGGS MTQSSVLNVK
     KGLVSPQRVQ SILSMLTTTS TSYLLLASLD VARKQLATKG HELIERTIQL ANYTREKINE
     IDDIYCVGKE ILGTKATFDY DPTKLIIPVY KLGISGYDVE NWLRNNYQIE VELSDLYNIL
     CIITPGDTKE DVDTLVHALK ELSTTVHINN KISNEKSHIL LPDIPVLALT PRDAFYSETE
     VVDFNDSAGR IIAEFIMVYP PGIPIFIPGE IISEDNLTYI KKNLEVGLPV QGPEDPSLKT
     IRVIKEHRAI K
//