ID   A0A1H8PBF5_9BACI        Unreviewed;       477 AA.
AC   A0A1H8PBF5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Lysine decarboxylase {ECO:0000313|EMBL:SEO39131.1};
GN   ORFNames=SAMN04488134_10712 {ECO:0000313|EMBL:SEO39131.1};
OS   Amphibacillus marinus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Amphibacillus.
OX   NCBI_TaxID=872970 {ECO:0000313|EMBL:SEO39131.1, ECO:0000313|Proteomes:UP000199300};
RN   [1] {ECO:0000313|EMBL:SEO39131.1, ECO:0000313|Proteomes:UP000199300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.10434 {ECO:0000313|EMBL:SEO39131.1,
RC   ECO:0000313|Proteomes:UP000199300};
RA   de Groot N.N.;
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}.
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DR   EMBL; FODJ01000007; SEO39131.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H8PBF5; -.
DR   STRING; 872970.SAMN04488134_10712; -.
DR   OrthoDB; 9815233at2; -.
DR   Proteomes; UP000199300; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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   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:UP000199300}.
FT   DOMAIN          8..300
FT                   /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT                   attachment site"
FT                   /evidence="ECO:0000259|Pfam:PF01276"
FT   DOMAIN          397..455
FT                   /note="Orn/Lys/Arg decarboxylase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03711"
SQ   SEQUENCE   477 AA;  53702 MW;  5605EE81CF09345C CRC64;
     MNRQLNKPIW EKLRHFQSNN PVSFHVPGHK NGKIMPSNEW FEFKSLLTYD LTELTGLDDL
     HNAEGIIEDA QQLAAEWFQA QKTYFLVNGS TVGNLAMILA TCGLNDQIIV QRNCHKSIIN
     GLELSGADPI FISPDYCNKH ERYTFPSLLT IKKAIDTYSN SKAILLTYPD YYGHTFALKE
     VVKYAHSHNM LVLIDEAHGV HFSLPNGTPL SAVELGADLV VQSAHKMAPA LTMTAFLHVG
     SDRVDASKLA YYLSALQSSS PSYLLLASLD LARYYLANLT VQEMAEIEQS VLTVRAVFAR
     VPLWRVLPQS DEDDFLKITL NVEACYSTRL IANFFEQEGI YPELVTDKHL LFVHGLASFT
     ALERLEATIE KLTSQLSFFP KRATIERKKL NFISPITHPV YSSLEMKDLD EELSAWGEAI
     GKVSAKTVIP YPPGIPVLLK GEQITEQHVQ YIQYLIDEQI NFQQSQIAEG VFVFKGE
//