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Database: UniProt
Entry: E1SDM4_PANVC
LinkDB: E1SDM4_PANVC
Original site: E1SDM4_PANVC 
ID   E1SDM4_PANVC            Unreviewed;       658 AA.
AC   E1SDM4;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 83.
DE   RecName: Full=Biosynthetic arginine decarboxylase {ECO:0000256|HAMAP-Rule:MF_01417};
DE            Short=ADC {ECO:0000256|HAMAP-Rule:MF_01417};
DE            EC=4.1.1.19 {ECO:0000256|HAMAP-Rule:MF_01417};
GN   Name=speA {ECO:0000256|HAMAP-Rule:MF_01417,
GN   ECO:0000313|EMBL:ADO10713.1};
GN   OrderedLocusNames=Pvag_2552 {ECO:0000313|EMBL:ADO10713.1};
OS   Pantoea vagans (strain C9-1) (Pantoea agglomerans (strain C9-1)).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea.
OX   NCBI_TaxID=712898 {ECO:0000313|EMBL:ADO10713.1, ECO:0000313|Proteomes:UP000006631};
RN   [1] {ECO:0000313|EMBL:ADO10713.1, ECO:0000313|Proteomes:UP000006631}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C9-1 {ECO:0000313|EMBL:ADO10713.1,
RC   ECO:0000313|Proteomes:UP000006631};
RX   PubMed=20952567; DOI=10.1128/JB.01122-10;
RA   Smits T.H., Rezzonico F., Kamber T., Goesmann A., Ishimaru C.A.,
RA   Stockwell V.O., Frey J.E., Duffy B.;
RT   "The genome sequence of the biocontrol agent Pantoea vagans strain C9-1.";
RL   J. Bacteriol. 192:6486-6487(2010).
CC   -!- FUNCTION: Catalyzes the biosynthesis of agmatine from arginine.
CC       {ECO:0000256|ARBA:ARBA00002257, ECO:0000256|HAMAP-Rule:MF_01417}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-arginine = agmatine + CO2; Xref=Rhea:RHEA:17641,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:32682,
CC         ChEBI:CHEBI:58145; EC=4.1.1.19; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01417};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|HAMAP-Rule:MF_01417};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|HAMAP-Rule:MF_01417, ECO:0000256|PIRSR:PIRSR001336-50};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; agmatine biosynthesis;
CC       agmatine from L-arginine: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01417}.
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC       SpeA subfamily. {ECO:0000256|ARBA:ARBA00008357, ECO:0000256|HAMAP-
CC       Rule:MF_01417}.
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DR   EMBL; CP002206; ADO10713.1; -; Genomic_DNA.
DR   RefSeq; WP_013358966.1; NC_014562.1.
DR   AlphaFoldDB; E1SDM4; -.
DR   KEGG; pva:Pvag_2552; -.
DR   eggNOG; COG1166; Bacteria.
DR   HOGENOM; CLU_027243_1_0_6; -.
DR   OMA; AVEYTQH; -.
DR   OrthoDB; 9802658at2; -.
DR   UniPathway; UPA00186; UER00284.
DR   Proteomes; UP000006631; Chromosome.
DR   GO; GO:0008792; F:arginine decarboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006527; P:arginine catabolic process; IEA:InterPro.
DR   GO; GO:0009446; P:putrescine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd06830; PLPDE_III_ADC; 1.
DR   Gene3D; 1.10.287.3440; -; 1.
DR   Gene3D; 1.20.58.930; -; 1.
DR   Gene3D; 3.20.20.10; Alanine racemase; 1.
DR   HAMAP; MF_01417; SpeA; 1.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR   InterPro; IPR040634; Arg_decarb_HB.
DR   InterPro; IPR041128; Arg_decarbox_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   NCBIfam; TIGR01273; speA; 1.
DR   PANTHER; PTHR43295; ARGININE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43295:SF9; BIOSYNTHETIC ARGININE DECARBOXYLASE; 1.
DR   Pfam; PF17810; Arg_decarb_HB; 1.
DR   Pfam; PF17944; Arg_decarbox_C; 1.
DR   Pfam; PF02784; Orn_Arg_deC_N; 1.
DR   PIRSF; PIRSF001336; Arg_decrbxlase; 1.
DR   PRINTS; PR01180; ARGDCRBXLASE.
DR   PRINTS; PR01179; ODADCRBXLASE.
DR   SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1.
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, ECO:0000256|HAMAP-
KW   Rule:MF_01417};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01417};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01417};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01417};
KW   Polyamine biosynthesis {ECO:0000256|ARBA:ARBA00023115, ECO:0000256|HAMAP-
KW   Rule:MF_01417}; Putrescine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01417};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01417,
KW   ECO:0000256|PIRSR:PIRSR001336-50};
KW   Spermidine biosynthesis {ECO:0000256|ARBA:ARBA00023066, ECO:0000256|HAMAP-
KW   Rule:MF_01417}.
FT   DOMAIN          101..367
FT                   /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02784"
FT   DOMAIN          391..478
FT                   /note="Arginine decarboxylase helical bundle"
FT                   /evidence="ECO:0000259|Pfam:PF17810"
FT   DOMAIN          606..655
FT                   /note="Arginine decarboxylase C-terminal helical"
FT                   /evidence="ECO:0000259|Pfam:PF17944"
FT   ACT_SITE        528
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT   BINDING         307..317
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01417"
FT   MOD_RES         127
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01417,
FT                   ECO:0000256|PIRSR:PIRSR001336-50"
SQ   SEQUENCE   658 AA;  74240 MW;  58D70A1693AEC7FC CRC64;
     MSDDMKNIKG SSAGEQGTLR SMQEVAMNDQ DASKMLRTYN IAWWGNNYYD VNELGHISVC
     PDPDRPDVRV DLARLVKERE AQGQRLPALF CFPQILQHRL RSINAAFKRA RESYGYKGDY
     FLVYPIKVNQ HKRVIESLIH SGEPLGLEAG SKAELMAVLA HAGQTRSVIV CNGYKDREYI
     RLALIGEKMG HKVYLVLEKM TEVRLVLEEA GRLNVVPRLG IRARLASQGS GKWQSSGGEK
     SKFGLSATQV LKLVEIMREA GRIDSLQLLH FHLGSQMSNI RDIATGVRES ARFYVELAKL
     GVNIKCFDVG GGLGVDYEGT RSQSDCSVNY GLNEYANNVI WAIGAACDEH GLDHPTVITE
     SGRAVTAHHT VLVSNIIGVE RNEFSEPETP DADAPRPILS MWETWQEMHE PDTRRSLREW
     LHDSQMDLSD IHTGYASGTY DLKQRSWAEQ LYLSICHYIQ QHLDPSNRAH RPIIDELQER
     MADKIYVNFS LFQSMPDAWG IDQLFPVLPL EGLNKKPERR AVLLDITCDS DGTIDHYVDG
     DGIATTMPMP QYDVDNPPML GFFMVGAYQE ILGNMHNLFG DTEAVDVYAR ENGEVEVQLS
     DEGDTVADML RYVQLDPNEL MALFRNQVQA SDLDDELRAQ FLEEFESGLY GYTYLEDE
//
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