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Database: UniProt
Entry: F3CF87_PSESG
LinkDB: F3CF87_PSESG
Original site: F3CF87_PSESG 
ID   F3CF87_PSESG            Unreviewed;       119 AA.
AC   F3CF87;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   SubName: Full=Arginine decarboxylase {ECO:0000313|EMBL:EGH17929.1};
DE            EC=4.1.1.19 {ECO:0000313|EMBL:EGH17929.1};
DE   Flags: Fragment;
GN   ORFNames=Pgy4_33781 {ECO:0000313|EMBL:EGH17929.1};
OS   Pseudomonas savastanoi pv. glycinea str. race 4.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=875330 {ECO:0000313|EMBL:EGH17929.1, ECO:0000313|Proteomes:UP000005466};
RN   [1] {ECO:0000313|EMBL:EGH17929.1, ECO:0000313|Proteomes:UP000005466}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=race 4 {ECO:0000313|Proteomes:UP000005466};
RX   PubMed=21799664; DOI=10.1371/journal.ppat.1002132;
RA   Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S.,
RA   Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.;
RT   "Dynamic evolution of pathogenicity revealed by sequencing and comparative
RT   genomics of 19 Pseudomonas syringae isolates.";
RL   PLoS Pathog. 7:E1002132-e1002132(2011).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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:EGH17929.1}.
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DR   EMBL; ADWY01002193; EGH17929.1; -; Genomic_DNA.
DR   AlphaFoldDB; F3CF87; -.
DR   Proteomes; UP000005466; Unassembled WGS sequence.
DR   GO; GO:0008792; F:arginine decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006527; P:arginine catabolic process; IEA:InterPro.
DR   GO; GO:0008295; P:spermidine biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.20.20.10; Alanine racemase; 1.
DR   InterPro; IPR002985; Arg_decrbxlase.
DR   InterPro; IPR022657; De-COase2_CS.
DR   InterPro; IPR022644; De-COase2_N.
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   SUPFAM; SSF51419; PLP-binding barrel; 1.
DR   PROSITE; PS00879; ODR_DC_2_2; 1.
PE   4: Predicted;
KW   Lyase {ECO:0000313|EMBL:EGH17929.1}.
FT   DOMAIN          7..119
FT                   /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02784"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EGH17929.1"
FT   NON_TER         119
FT                   /evidence="ECO:0000313|EMBL:EGH17929.1"
SQ   SEQUENCE   119 AA;  13047 MW;  0D17777796F255F9 CRC64;
     EAKVERVIEE AAELKVAPQV GLRVRLSSLA SSKWADTGGE KSKFGLSAAQ LLSVVERFRK
     AGLDQGIRLL HFHMGSQIAN LADYQHGFKE AIRYYGELRK LGLPVDYIDV GGGLGVDYD
//
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