ID   A0A1S2QSG2_9BACI        Unreviewed;       491 AA.
AC   A0A1S2QSG2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=Arginine decarboxylase {ECO:0000313|EMBL:OIK09054.1};
GN   ORFNames=BIV59_18115 {ECO:0000313|EMBL:OIK09054.1};
OS   Bacillus sp. MUM 13.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1678001 {ECO:0000313|EMBL:OIK09054.1, ECO:0000313|Proteomes:UP000180199};
RN   [1] {ECO:0000313|EMBL:OIK09054.1, ECO:0000313|Proteomes:UP000180199}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MUM 13 {ECO:0000313|EMBL:OIK09054.1,
RC   ECO:0000313|Proteomes:UP000180199};
RA   Lee L.-H., Ser H.-L.;
RT   "Genome sequence of Bacillus sp. MUM 13.";
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}.
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:OIK09054.1}.
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; MLYQ01000088; OIK09054.1; -; Genomic_DNA.
DR   RefSeq; WP_071352864.1; NZ_MLYQ01000088.1.
DR   AlphaFoldDB; A0A1S2QSG2; -.
DR   Proteomes; UP000180199; 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:UP000180199}.
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;  53744 MW;  B157A2101C3C5F52 CRC64;
     MSQYETPLFT GLINHAKKNP IQFHIPGHKK GQGIDPEFRN FIGENALSID LINIAPLDDL
     HQPKGIIKQA QDLAAEAFGA DHTFFSVQGT SGAIMTMVMA VCGPGDKIIV PRNVHKSVMS
     AIVFSGAVPI FIHPEIDKEL GISHGITTES VEKALEQNPD AKGLLVINPT YFGVSADLKK
     IVEIAHSYSV PVLVDEAHGV HIHFHEGLPM SAMQAGADMA ATSVHKLGGS LTQSSVLNVK
     EGLVSSNHVQ SILSMLTTTS TSYILLASLD VARKRLATEG RELIDKAIKL ADHIRYEVNT
     IPKLTCIGRE ILGSKATFDY DPTKLIISVK ELGISGYDVE KWLREKHNIE VELSDLYNIL
     CLVTTGDTET EAEILISALR DLAEEFNHYQ GENQEISEVM LPDIPLLALT PRDAFYASTE
     VVPIEESAGR IIAEFIMVYP PGIPIFIPGE IITEENIAYI KKNIEVGLPV QGPEDSELKN
     LRVIKERKAI I
//