ID Q48DK1_PSE14 Unreviewed; 637 AA. AC Q48DK1; DT 13-SEP-2005, integrated into UniProtKB/TrEMBL. DT 13-SEP-2005, sequence version 1. DT 27-MAR-2024, entry version 116. 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:AAZ33811.1}; GN OrderedLocusNames=PSPPH_4424 {ECO:0000313|EMBL:AAZ33811.1}; OS Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6) OS (Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6)). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=264730 {ECO:0000313|EMBL:AAZ33811.1, ECO:0000313|Proteomes:UP000000551}; RN [1] {ECO:0000313|EMBL:AAZ33811.1, ECO:0000313|Proteomes:UP000000551} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1448A / Race 6 {ECO:0000313|Proteomes:UP000000551}; RX PubMed=16159782; DOI=10.1128/JB.187.18.6488-6498.2005; RA Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R., RA Brinkac L.M., Daugherty S.C., Deboy R., Durkin A.S., Giglio M.G., RA Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S., Crabtree J., Creasy T., RA Davidsen T., Haft D.H., Zafar N., Zhou L., Halpin R., Holley T., Khouri H., RA Feldblyum T., White O., Fraser C.M., Chatterjee A.K., Cartinhour S., RA Schneider D.J., Mansfield J., Collmer A., Buell C.R.; RT "Whole-genome sequence analysis of Pseudomonas syringae pv. phaseolicola RT 1448A reveals divergence among pathovars in genes involved in virulence and RT transposition."; RL J. Bacteriol. 187:6488-6498(2005). 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, ECO:0000256|HAMAP- CC Rule:MF_01417}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|ARBA:ARBA00001933, ECO:0000256|HAMAP- CC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000058; AAZ33811.1; -; Genomic_DNA. DR RefSeq; WP_004666294.1; NC_005773.3. DR AlphaFoldDB; Q48DK1; -. DR GeneID; 69861436; -. DR KEGG; psp:PSPPH_4424; -. DR eggNOG; COG1166; Bacteria. DR HOGENOM; CLU_027243_1_0_6; -. DR UniPathway; UPA00186; UER00284. DR Proteomes; UP000000551; 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: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; IPR022657; De-COase2_CS. DR InterPro; IPR022644; De-COase2_N. 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; PS00879; ODR_DC_2_2; 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}; 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 100..350 FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal" FT /evidence="ECO:0000259|Pfam:PF02784" FT DOMAIN 376..458 FT /note="Arginine decarboxylase helical bundle" FT /evidence="ECO:0000259|Pfam:PF17810" FT DOMAIN 586..635 FT /note="Arginine decarboxylase C-terminal helical" FT /evidence="ECO:0000259|Pfam:PF17944" FT ACT_SITE 508 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50" FT BINDING 290..300 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01417" FT MOD_RES 110 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01417, FT ECO:0000256|PIRSR:PIRSR001336-50" SQ SEQUENCE 637 AA; 71396 MW; 1E9FCEBD3392A87C CRC64; MSVRRTRKDD GSQWTVADSR SVYGIRHWGA GYFAINEAGR VEVRPNGPDS SPIDLYEQVD NLRKSGLSLP LLVRFPDILQ DRVRQLTGAF DSNIARLEYQ SQYTALYPIK VNQQEAVVEN IIATQNVSIG LEAGSKPELM AVLALAPKGG TIVCNGYKDR EFIRLALMGQ KLGHNVFIVI EKESEVELVI EEAAELKVAP QVGLRVRLSS LASSKWADTG GEKSKFGLSA AQLLSVVERF RKAGLDQGIR LLHFHMGSQI ANLADYQHGF KEAIRYYGEL RKLGLPVDYI DVGGGLGVDY DGTHSRNASS INYDMDDYAG VVVGMLKEFC DAQSLPHPHI FSESGRSLTA HHAMLVVQVT DVEKHNDEVP EISDKESLPE TVQWLVDLLG PTDIEMVTET YWRATHYMSD IATQYADGKI SLAEKALGEQ CYFAVCRRLY NSLKARQRSH RQVLDELNDK LADKYICNFS VFQSLPDTWA IGQVLPILPL HRLDEEPVRR AVLQDLTCDS DGKIKQYVDE QSIETSMPVH SLNEGEDYLL GIFLVGAYQE ILGDMHNLFG DTDSVNIYQN PDGSVYHAGI ETHDTIEDML RYVHLSPEEL MTHYRDKVAS AKITPRERTY FLDALRLGLT RSSYLSS //