ID G5SGN1_SALET Unreviewed; 259 AA.
AC G5SGN1;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=arginine decarboxylase {ECO:0000256|ARBA:ARBA00012426};
DE EC=4.1.1.19 {ECO:0000256|ARBA:ARBA00012426};
GN ORFNames=LTSEWAN_4710 {ECO:0000313|EMBL:EHC99946.1};
OS Salmonella enterica subsp. enterica serovar Wandsworth str. A4-580.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=913086 {ECO:0000313|EMBL:EHC99946.1, ECO:0000313|Proteomes:UP000003536};
RN [1] {ECO:0000313|EMBL:EHC99946.1, ECO:0000313|Proteomes:UP000003536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A4-580 {ECO:0000313|EMBL:EHC99946.1,
RC ECO:0000313|Proteomes:UP000003536};
RX PubMed=21859443; DOI=10.1186/1471-2164-12-425;
RA den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., Ranieri M.L.,
RA Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., Brown S., Bolchacova E.,
RA Furtado M.R., Wiedmann M.;
RT "Genome sequencing reveals diversification of virulence factor content and
RT possible host adaptation in distinct subpopulations of Salmonella
RT enterica.";
RL BMC Genomics 12:425-425(2011).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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-II family.
CC SpeA subfamily. {ECO:0000256|ARBA:ARBA00008357}.
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:EHC99946.1}.
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DR EMBL; AFCX01001540; EHC99946.1; -; Genomic_DNA.
DR AlphaFoldDB; G5SGN1; -.
DR PATRIC; fig|913086.3.peg.3623; -.
DR Proteomes; UP000003536; Unassembled WGS sequence.
DR GO; GO:0008792; F:arginine decarboxylase activity; IEA:InterPro.
DR GO; GO:0006527; P:arginine catabolic process; IEA:InterPro.
DR GO; GO:0009446; P:putrescine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.10; Alanine racemase; 1.
DR InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR InterPro; IPR002985; Arg_decrbxlase.
DR InterPro; IPR022644; De-COase2_N.
DR InterPro; IPR022653; De-COase2_pyr-phos_BS.
DR InterPro; IPR000183; Orn/DAP/Arg_de-COase.
DR InterPro; IPR029066; PLP-binding_barrel.
DR PANTHER; PTHR43295; ARGININE DECARBOXYLASE; 1.
DR PANTHER; PTHR43295:SF9; BIOSYNTHETIC ARGININE DECARBOXYLASE; 1.
DR Pfam; PF02784; Orn_Arg_deC_N; 1.
DR PRINTS; PR01180; ARGDCRBXLASE.
DR PRINTS; PR01179; ODADCRBXLASE.
DR SUPFAM; SSF51419; PLP-binding barrel; 1.
DR PROSITE; PS00878; ODR_DC_2_1; 1.
PE 3: Inferred from homology;
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Putrescine biosynthesis {ECO:0000256|ARBA:ARBA00023023};
KW Spermidine biosynthesis {ECO:0000256|ARBA:ARBA00023066}.
FT DOMAIN 74..257
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
SQ SEQUENCE 259 AA; 29000 MW; A68BD5108BC0B39C CRC64;
MSSQEASKML RTYNIAWWGN NYYDVNELGH ISVCPDPDVP EARVDLAKLV KAREAQGQRL
PALFCFPQIL QHRLRSINAA FKRARESYGY NGDYFLVYPI KVNQHRRVIE SLIHSGEPLG
LEAGSKAELM AVLAHAGMTR SVIVCNGYKD REYIRLALIG EKMGHKVYLV IEKMSEIAIV
LEEAERLNVV PRLGVRARLA SQGSGKWQSS GGEKSKFGLA ATQVLQLVET LRDAGRLDSL
QLLHFHLGSQ MANIRDIAL
//
