ID A0A1R4HSJ9_9MICO Unreviewed; 513 AA.
AC A0A1R4HSJ9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Arginine decarboxylase / Lysine decarboxylase {ECO:0000313|EMBL:SJN10507.1};
DE EC=4.1.1.18 {ECO:0000313|EMBL:SJN10507.1};
DE EC=4.1.1.19 {ECO:0000313|EMBL:SJN10507.1};
GN ORFNames=FM113_09290 {ECO:0000313|EMBL:SJN10507.1};
OS Leucobacter sp. 7(1).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leucobacter.
OX NCBI_TaxID=1255613 {ECO:0000313|EMBL:SJN10507.1, ECO:0000313|Proteomes:UP000195513};
RN [1] {ECO:0000313|EMBL:SJN10507.1, ECO:0000313|Proteomes:UP000195513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7(1) {ECO:0000313|Proteomes:UP000195513};
RA Peterson S.W.;
RL Submitted (FEB-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}.
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DR EMBL; FUID01000050; SJN10507.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R4HSJ9; -.
DR OrthoDB; 9815233at2; -.
DR Proteomes; UP000195513; Unassembled WGS sequence.
DR GO; GO:0008792; F:arginine decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0008923; F:lysine decarboxylase activity; IEA:UniProtKB-EC.
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: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.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:SJN10507.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000195513}.
FT DOMAIN 17..316
FT /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT attachment site"
FT /evidence="ECO:0000259|Pfam:PF01276"
FT DOMAIN 434..489
FT /note="Orn/Lys/Arg decarboxylase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03711"
SQ SEQUENCE 513 AA; 53603 MW; 464CE479086304BA CRC64;
MSPQQAPPSQ DAQHLAPYAD ALEAHRARSG LRFMIPGHAA GGAGGSDRLR DFLGARALEL
DIPQLVEGID LGANNAFDQA RRLAASAWGA RTSWFLTNGA SQGNRMALQA IAALGDRVLV
QRSCHSSVYD GLVMSGARPE YIFPEFDPHH GIAHGITPET AERALSEAAA EGQPFAALVL
VSPSYFGVVS DIAAIATSCH NYGAALIVDG SWGAHFGFHP NLPESPTRQG ADVVLTSVHK
LGGSLTQTAF LHLCDTPVGA QLEPALDAAY RLTESTSLNS LLLASLDIAR AELATGSEAM
GAALASAAEL RELVAASPGL RLAEPDFLAH PGSTSIDPLH VSIDVRGRDV SGPELKSRLA
SAEPPVFVEI ASPTTIVALI GPRSSPNVTG LMAAIDACAP PQPRDTRADE LSFATPDTDD
LSRLPTAPAP GERVLTPREA YLARSESVPA TAAEGRVSAA MLAAYPPGIP NAVPGERLTA
ELITYLRETA ALPGSYIRGA EDPEVTHIRV LLE
//
